{"title":"Evaluation of automated cell disruptor methods for oomycetous and ascomycetous model organisms","authors":"T. Kasuga, Mai Bui","doi":"10.4148/1941-4765.1065","DOIUrl":"https://doi.org/10.4148/1941-4765.1065","url":null,"abstract":"","PeriodicalId":12490,"journal":{"name":"Fungal Genetics Reports","volume":"65 1","pages":"4-13"},"PeriodicalIF":0.0,"publicationDate":"2011-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87162025","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Here we report the construction and application of a range of expression plasmids designed to facilitate livecell imaging of F-actin dynamics in filamentous fungi simultaneously with other, preferably GFP-tagged fusion proteins. Pros and cons of the use of three different red fluorescent proteins (RFPs), two different promoters and three different selection markers are addressed. Creative Commons License This work is licensed under a Creative Commons Attribution-Share Alike 4.0 License. This regular paper is available in Fungal Genetics Reports: http://newprairiepress.org/fgr/vol57/iss1/4 8 Fungal Genetics Reports A versatile set of Lifeact-RFP expression plasmids for live-cell imaging of F-actin in filamentous fungi Alexander Lichius and Nick D. Read Fungal Cell Biology Group, Institute of Cell Biology, University of Edinburgh, Rutherford Building, Edinburgh EH9 3JR, UK; Alex@fungalcell.org Fungal Genetics Reports 57:8-14 Here we report the construction and application of a range of expression plasmids designed to facilitate live-cell imaging of F-actin dynamics in filamentous fungi simultaneously with other, preferably GFP-tagged fusion proteins. Pros and cons of the use of three different red fluorescent proteins (RFPs), two different promoters and three different selection markers are addressed. Live-cell imaging of F-actin dynamics is possible in a wide range of eukaryotes. Lifeact is a 17 aa peptide derived from the actin-binding protein 140 (Abp140) of S. cerevisiae which specifically binds to filamentous actin (F-actin) (Riedl et al., 2008). Functionality of green fluorescent Lifeact reporters (Lifeact-GFP) for the visualisation of F-actin structures in living cells has so far been documented for three of the four eukaryotic phyla, including yeasts and filamentous fungi (Berepiki et al., 2010; Böhmer et al., 2009; Coffman et al., 2009; Delgado-Álvarez et al., 2010; Riedl et al., 2008), plants (Era et al., 2009; Smertenko et al., 2010; Vidali et al., 2009), and mammals (Estecha et al., 2009; Riedl et al., 2008; Riedl et al., 2010). The application of Lifeact-GFP in filamentous fungi has been pioneered in the ascomycete Neurospora crassa (Berepiki et al., 2010; Delgado-Álvarez et al., 2010), and is currently being adopted for the use in numerous other fungal species. In basidiomycetes, however, labelling properties of Lifeact appear to be restricted to the visualization of septal rings, as F-actin cables and patches have so far not been explicitly reported (Böhmer et al., 2009). Lifeact-GFP reporters work equally well in fungi that use the CUG codon for serine and not leucine, such as Candida sp. (Kawaguchi et al., 1989), once they have been codon corrected, (E. Epp, McGill Univ. Montreal, pers.comm.). Why RFP and which one? The most widely used fluorescent reporter for live-cell imaging analyses of protein dynamics in filamentous fungi is GFP. To allow simultaneous observation of F-actin with any other GFP-tagged protein, the development o
在这里，我们报道了一系列表达质粒的构建和应用，旨在促进丝状真菌中f -肌动蛋白动力学的活细胞成像，同时与其他，最好是gfp标记的融合蛋白。讨论了使用三种不同的红色荧光蛋白(rfp)、两种不同的启动子和三种不同的选择标记的利弊。本作品采用知识共享署名-相同方式共享4.0许可协议。Alexander Lichius和Nick D. Read真菌细胞生物学小组，爱丁堡大学细胞生物学研究所，卢瑟福大楼，爱丁堡EH9 3JR，英国;Alex@fungalcell.org真菌遗传学报告57:8-14在这里，我们报道了一系列表达质粒的构建和应用，旨在促进丝状真菌中f -肌动蛋白动态的活细胞成像，同时与其他，最好是gfp标记的融合蛋白。讨论了使用三种不同的红色荧光蛋白(rfp)、两种不同的启动子和三种不同的选择标记的利弊。在广泛的真核生物中，f -肌动蛋白动力学的活细胞成像是可能的。Lifeact是从酿酒酵母的肌动蛋白结合蛋白140 (Abp140)中提取的一种17aa肽，它特异性地与丝状肌动蛋白(F-actin)结合(Riedl et al.， 2008)。绿色荧光Lifeact报告蛋白(Lifeact- gfp)对活细胞中f -肌动蛋白结构可视化的功能迄今已在四种真核生物门中的三种中得到证实，包括酵母和丝状真菌(Berepiki et al.， 2010;Böhmer等，2009;Coffman et al.， 2009;Delgado-Álvarez et al.， 2010;Riedl et al.， 2008)，植物(Era et al.， 2009;Smertenko et al.， 2010;Vidali et al.， 2009)和哺乳动物(Estecha et al.， 2009;Riedl et al.， 2008;Riedl et al.， 2010)。Lifeact-GFP在丝状真菌中的应用已在子囊菌粗神经孢子菌(Berepiki et al.， 2010;Delgado-Álvarez et al.， 2010)，目前正被用于许多其他真菌物种。然而，在担子菌中，Lifeact的标记特性似乎仅限于间隔环的可视化，因为f -肌动蛋白电缆和斑块迄今尚未明确报道(Böhmer et al.， 2009)。Lifeact-GFP报告器在使用CUG密码子表示丝氨酸而不是亮氨酸的真菌中同样有效，如念珠菌sp. (Kawaguchi等人，1989)，一旦它们被密码子纠正，(E. Epp, McGill university . Montreal, pers.com)。为什么是RFP，哪一个?用于丝状真菌蛋白动态活细胞成像分析的最广泛使用的荧光报告蛋白是绿色荧光蛋白。为了同时观察f -肌动蛋白与任何其他gfp标记的蛋白质，需要开发一种标记为不同颜色的Lifeact探针(Riedl等人，2008)。由于绿色和红色发射信号可以在光谱上很好地分离，并且具有相应激发和发射检测设置的荧光显微镜广泛可用，我们的目标是生成功能性Lifeact-RFP报告结构。我们对丝状模型真菌粗神经孢子菌采用的第一个红色荧光Lifeact探针是Lifeact- tdtomato (Roca等，2010)。虽然Lifeact-tdTomato可靠地标记了f-肌动蛋白斑块、电缆和间隔环(图1)，但本文偶尔会产生额外的环状结构(直径约1-2 μm，图1B和C)，我们认为这些结构可能是通过f-肌动蛋白的自发自组装形成的，通过与Lifeact-tdTomato构建体和天然间隔蛋白的相互作用而不稳定。先前的研究表明，由于空间位阻，mRFP和tdTomato融合构建体无法正确定位微管和连接蛋白(Shaner等，2004;Shaner et al.， 2008)。一些rfp的这一尚未被充分理解的特性可能增强了过度表达的Lifeact-tdTomato融合结构的错误定位产物，从而导致不稳定的f -肌动蛋白形成这些细胞质环。有趣的是，据报道，在哺乳动物细胞(Kinoshita et al.， 2002)和麦氏黑木耳(Ustilago maydis)单倍体细胞(Böhmer et al.， 2009)中，Latrunculin A也能形成类似的结构。这些环在N. crassa中的出现是通过将tdTomato交换为单体红色荧光蛋白TagRFP来解决的(Shaner et al.， 2008)。图1所示。lifeact - rfp标签的f -肌动蛋白电缆，补丁和环。(A)两个表达lifeacttagfp的融合wt细胞。f -肌动蛋白索在上细胞的孢子体中伸展，而肌动蛋白斑块分布在下细胞的表面。 密集排列的肌动蛋白索位于细胞融合位点(箭头)，并在隔膜形成之前凝聚成肌动蛋白环(箭头)。(B至D)表达Lifeact-tdTomato的wt分生孢子样例。(B)肌动蛋白索与胚管长轴对齐的分生孢子胚芽。细胞质中有一个非常明亮的荧光环(箭头)，但与任何已知的细胞结构无关。类似的环在其他模型系统中也有描述，可能是Lifeact-tdTomato结构与天然septin自发自组装的产物(详见文本)。此外，融合结构的液泡积累产生了轻微的人工背景荧光。(C)细胞内不同位置有明亮荧光环的两个融合胚。(D) CAT归巢过程中的分生孢子(Read et al.， 2009)，在较小的胚芽(箭头)顶端有大量的肌动蛋白斑块和索。孢子颈部皮层肌动蛋白环的形成再次用箭头表示。所有图像显示反卷积z堆栈的最大强度投影。比例尺，5 μm。新草原出版社2017年出版
{"title":"A versatile set of Lifeact-RFP expression plasmids for live-cell imaging of F-actin in filamentous fungi","authors":"Alexander Lichius, N. Read","doi":"10.4148/1941-4765.1070","DOIUrl":"https://doi.org/10.4148/1941-4765.1070","url":null,"abstract":"Here we report the construction and application of a range of expression plasmids designed to facilitate livecell imaging of F-actin dynamics in filamentous fungi simultaneously with other, preferably GFP-tagged fusion proteins. Pros and cons of the use of three different red fluorescent proteins (RFPs), two different promoters and three different selection markers are addressed. Creative Commons License This work is licensed under a Creative Commons Attribution-Share Alike 4.0 License. This regular paper is available in Fungal Genetics Reports: http://newprairiepress.org/fgr/vol57/iss1/4 8 Fungal Genetics Reports A versatile set of Lifeact-RFP expression plasmids for live-cell imaging of F-actin in filamentous fungi Alexander Lichius and Nick D. Read Fungal Cell Biology Group, Institute of Cell Biology, University of Edinburgh, Rutherford Building, Edinburgh EH9 3JR, UK; Alex@fungalcell.org Fungal Genetics Reports 57:8-14 Here we report the construction and application of a range of expression plasmids designed to facilitate live-cell imaging of F-actin dynamics in filamentous fungi simultaneously with other, preferably GFP-tagged fusion proteins. Pros and cons of the use of three different red fluorescent proteins (RFPs), two different promoters and three different selection markers are addressed. Live-cell imaging of F-actin dynamics is possible in a wide range of eukaryotes. Lifeact is a 17 aa peptide derived from the actin-binding protein 140 (Abp140) of S. cerevisiae which specifically binds to filamentous actin (F-actin) (Riedl et al., 2008). Functionality of green fluorescent Lifeact reporters (Lifeact-GFP) for the visualisation of F-actin structures in living cells has so far been documented for three of the four eukaryotic phyla, including yeasts and filamentous fungi (Berepiki et al., 2010; Böhmer et al., 2009; Coffman et al., 2009; Delgado-Álvarez et al., 2010; Riedl et al., 2008), plants (Era et al., 2009; Smertenko et al., 2010; Vidali et al., 2009), and mammals (Estecha et al., 2009; Riedl et al., 2008; Riedl et al., 2010). The application of Lifeact-GFP in filamentous fungi has been pioneered in the ascomycete Neurospora crassa (Berepiki et al., 2010; Delgado-Álvarez et al., 2010), and is currently being adopted for the use in numerous other fungal species. In basidiomycetes, however, labelling properties of Lifeact appear to be restricted to the visualization of septal rings, as F-actin cables and patches have so far not been explicitly reported (Böhmer et al., 2009). Lifeact-GFP reporters work equally well in fungi that use the CUG codon for serine and not leucine, such as Candida sp. (Kawaguchi et al., 1989), once they have been codon corrected, (E. Epp, McGill Univ. Montreal, pers.comm.). Why RFP and which one? The most widely used fluorescent reporter for live-cell imaging analyses of protein dynamics in filamentous fungi is GFP. To allow simultaneous observation of F-actin with any other GFP-tagged protein, the development o","PeriodicalId":12490,"journal":{"name":"Fungal Genetics Reports","volume":"84 1","pages":"8-14"},"PeriodicalIF":0.0,"publicationDate":"2010-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80560788","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
R. Schnittker, Senthilkumar Sivagurunathan, M. Plamann
{"title":"Work in the dark to harvest large liquid-grown cultures","authors":"R. Schnittker, Senthilkumar Sivagurunathan, M. Plamann","doi":"10.4148/1941-4765.1069","DOIUrl":"https://doi.org/10.4148/1941-4765.1069","url":null,"abstract":"","PeriodicalId":12490,"journal":{"name":"Fungal Genetics Reports","volume":"16 1","pages":"7"},"PeriodicalIF":0.0,"publicationDate":"2010-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81954269","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Most heterothallic basidiomycetes use small lipopeptide pheromones as part of mate recognition. Schizophyllum commune has scores of pheromones that must be specifically recognized by mating receptors. A correlation between a phenylalanine residue near the C-terminus of several pheromones and the ability of those pheromones to activate receptor Bar4 was recognized. We hypothesized that the phenylalanine residue would be critical for Bar4 activation and tested the hypothesis by making site-directed mutant pheromones and testing these pheromone variants in matings. The data support the hypothesis and add to our understanding of which amino acid residues within pheromones are critical for specific recognition by pheromone receptors. Creative Commons License This work is licensed under a Creative Commons Attribution-Share Alike 4.0 License. This regular paper is available in Fungal Genetics Reports: http://newprairiepress.org/fgr/vol57/iss1/2 4 Fungal Genetics Reports A carboxy-subterminal aromatic residue in Schizophyllum commune mating pheromones controls specific recognition by Bar4 receptor Thomas Fowler Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, IL 62026; tfowler@siue.edu Fungal Genetics Reports 57:4-6 Most heterothallic basidiomycetes use small lipopeptide pheromones as part of mate recognition. Schizophyllum commune has scores of pheromones that must be specifically recognized by mating receptors. A correlation between a phenylalanine residue near the Cterminus of several pheromones and the ability of those pheromones to activate receptor Bar4 was recognized. We hypothesized that the phenylalanine residue would be critical for Bar4 activation and tested the hypothesis by making site-directed mutant pheromones and testing these pheromone variants in matings. The data support the hypothesis and add to our understanding of which amino acid residues within pheromones are critical for specific recognition by pheromone receptors. Many of the Agaricomycotina fungi express quite a few mating pheromones and seven-transmembrane-domain pheromone receptors (most recently reviewed by Raudaskoski and Kothe, 2010). A large number of lipopeptide mating pheromones are coded species-wide by Schizophyllum commune, but any individual has genes for only a small subset of the species’ estimated 80–100 pheromones. More than twenty of the genes that encode these pheromones have been cloned and sequenced (for list and references, see Table 3 in Fowler et al., 2004). One attempt at classifying these pheromones placed them into five groups according to similarity of the predicted mature pheromones’ amino acid sequences (Fowler et al., 2004). The subsets of receptors activated by the pheromones follow a pattern that closely correlates with pheromone groups arranged by sequence similarity. Three pheromone groups (III, IV,V) arranged by similarity activate three completely distinct sets of receptors. The remaining two pheromo
大多数担子菌使用小脂肽信息素作为配偶识别的一部分。裂叶植物群落有大量的信息素，这些信息素必须被交配受体特异性识别。一些信息素c端附近的苯丙氨酸残基与这些信息素激活受体Bar4的能力之间存在相关性。我们假设苯丙氨酸残基对Bar4的激活至关重要，并通过制造定点突变信息素和在交配中测试这些信息素变体来验证这一假设。这些数据支持了这一假设，并增加了我们对信息素中哪些氨基酸残基对信息素受体的特异性识别至关重要的理解。本作品采用知识共享署名-相同方式共享4.0许可协议。这篇常规的论文可在真菌遗传学报告:http://newprairiepress.org/fgr/vol57/iss1/2 4真菌遗传学报告Schizophyllum commune交配信息素中的羧基亚末端芳香残基控制Bar4受体的特异性识别;tfowler@siue.edu真菌遗传学报告57:4-6大多数异thallic担子菌使用小脂肽信息素作为配偶识别的一部分。裂叶植物群落有大量的信息素，这些信息素必须被交配受体特异性识别。在几种信息素的Cterminus附近的苯丙氨酸残基与这些信息素激活受体Bar4的能力之间存在相关性。我们假设苯丙氨酸残基对Bar4的激活至关重要，并通过制造定点突变信息素和在交配中测试这些信息素变体来验证这一假设。这些数据支持了这一假设，并增加了我们对信息素中哪些氨基酸残基对信息素受体的特异性识别至关重要的理解。许多Agaricomycotina真菌表达相当多的交配信息素和七种跨膜域信息素受体(Raudaskoski和Kothe, 2010年最近进行了综述)。在裂叶植物群落中，大量的脂肽交配信息素在物种范围内被编码，但任何个体都只有物种估计的80-100个信息素的一小部分基因。编码这些信息素的基因有20多个已被克隆和测序(列表和参考文献见Fowler et al.， 2004的表3)。根据预测的成熟信息素氨基酸序列的相似性，将这些信息素分为五组(Fowler et al.， 2004)。被信息素激活的受体亚群遵循一种模式，这种模式与按序列相似性排列的信息素群密切相关。按相似性排列的三个信息素组(III, IV,V)激活三组完全不同的受体。剩下的两个信息素组(I和II)也有相应的受体，它们只被各自组内的信息素明显激活，只有一个例外:信息素受体Bar4被来自I族的信息素Bap3(1)和来自II族的信息素Bap3(3)和Bbp2(6)激活(表1)。比较I族和II族信息素的氨基酸序列发现，除了信息素Bap3(1)在羧基亚末端具有苯丙氨酸(F)外，所有I族信息素在羧基亚末端都含有色氨酸(W)，并能激活受体Bar4。这两种II族信息素在羧基亚末端位置也有F。在已鉴定的I和II类的7种野生型信息素中，羧基亚末端位置为F的信息素可以激活Bar4，而羧基亚末端位置为W的信息素不能激活Bar4 (Fowler et al.， 2004)。我们想知道单个F残基是否可能是Bar4识别为激活配体的关键。在真菌脂肽交配信息素内的其他关键氨基酸残基测试中，单个氨基酸是至关重要的。信息素中的一个氨基酸可以决定受体激活或失败，或者在不失去原始信息素活性的情况下与不同的受体产生活性(Olesnicky等人，2000;Fowler et al.， 2001)。我们感兴趣的是控制信息素和信息素受体相互作用的规则和模式。表1。野生型和突变型信息素序列和活性组名称预测信息素受体激活野生型信息素I Bap3(1) ERVGTGGTATAFC Bar2, Bar4, Bar5 II Bap3(3) ERHGSGNMTYFC Bar4, Bar7, Bbr8 II Bbp2(6) EREGDGNMTYFC Bar4, Bar7, Bbr8 I Bap1(1)r EREGGSDCTAWC Bar2, Bar4, Bar5, Bar6突变型信息素I Bap3(1)F54Y ERVGTGGTATAYC Bar2, Bar4, Bar5 I Bap3(1)F54W ERVGTGGTATAYC Bar2, Bar5 I Bap1(1)rW30F EREGGSDCTAFC Bar2, Bar3, Bar4, Bar5
{"title":"A carboxy-subterminal aromatic residue in Schizophyllum commune mating pheromones controls specific recognition by Bar4 receptor","authors":"T. Fowler","doi":"10.4148/1941-4765.1068","DOIUrl":"https://doi.org/10.4148/1941-4765.1068","url":null,"abstract":"Most heterothallic basidiomycetes use small lipopeptide pheromones as part of mate recognition. Schizophyllum commune has scores of pheromones that must be specifically recognized by mating receptors. A correlation between a phenylalanine residue near the C-terminus of several pheromones and the ability of those pheromones to activate receptor Bar4 was recognized. We hypothesized that the phenylalanine residue would be critical for Bar4 activation and tested the hypothesis by making site-directed mutant pheromones and testing these pheromone variants in matings. The data support the hypothesis and add to our understanding of which amino acid residues within pheromones are critical for specific recognition by pheromone receptors. Creative Commons License This work is licensed under a Creative Commons Attribution-Share Alike 4.0 License. This regular paper is available in Fungal Genetics Reports: http://newprairiepress.org/fgr/vol57/iss1/2 4 Fungal Genetics Reports A carboxy-subterminal aromatic residue in Schizophyllum commune mating pheromones controls specific recognition by Bar4 receptor Thomas Fowler Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, IL 62026; tfowler@siue.edu Fungal Genetics Reports 57:4-6 Most heterothallic basidiomycetes use small lipopeptide pheromones as part of mate recognition. Schizophyllum commune has scores of pheromones that must be specifically recognized by mating receptors. A correlation between a phenylalanine residue near the Cterminus of several pheromones and the ability of those pheromones to activate receptor Bar4 was recognized. We hypothesized that the phenylalanine residue would be critical for Bar4 activation and tested the hypothesis by making site-directed mutant pheromones and testing these pheromone variants in matings. The data support the hypothesis and add to our understanding of which amino acid residues within pheromones are critical for specific recognition by pheromone receptors. Many of the Agaricomycotina fungi express quite a few mating pheromones and seven-transmembrane-domain pheromone receptors (most recently reviewed by Raudaskoski and Kothe, 2010). A large number of lipopeptide mating pheromones are coded species-wide by Schizophyllum commune, but any individual has genes for only a small subset of the species’ estimated 80–100 pheromones. More than twenty of the genes that encode these pheromones have been cloned and sequenced (for list and references, see Table 3 in Fowler et al., 2004). One attempt at classifying these pheromones placed them into five groups according to similarity of the predicted mature pheromones’ amino acid sequences (Fowler et al., 2004). The subsets of receptors activated by the pheromones follow a pattern that closely correlates with pheromone groups arranged by sequence similarity. Three pheromone groups (III, IV,V) arranged by similarity activate three completely distinct sets of receptors. The remaining two pheromo","PeriodicalId":12490,"journal":{"name":"Fungal Genetics Reports","volume":"4 1","pages":"4-6"},"PeriodicalIF":0.0,"publicationDate":"2010-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82380720","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A procedure is described for isolation and purification of four high-molecular mass stress-responsive proteins from the same starting material. This regular paper is available in Fungal Genetics Reports: https://newprairiepress.org/fgr/vol56/iss1/4 8 Fungal Genetics Reports A procedure for parallel purification of four stress-related Neurospora proteins in their native state. M. Kapoor. Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada Fungal Genetics Reports 65:8-11 A procedure is described for isolation and purification of four high-molecular mass stress-responsive proteins from the same starting material. Proteins are the major components determining cellular growth, metabolism, regulation, repair, homeostatic mechanisms, differentiation, organogenesis, response to environmental factors and ultimately survival. Extensive protein networks form the basis of interlocking metabolic pathways and their regulatory circuits in the eukaryotic and prokaryotic cells, involving transient interactions among a large, overwhelming array of actors. Availability of purified proteins in their native state is critical on account of the universal interest in unraveling how proteins function in their endogenous intracellular environment. With the rapid progress in genomics and availability of an ever increasing number of crystal structures, an understanding of the molecular basis of interactions of proteins with ligands, substrates and regulatory molecules is achievable. Structural studies, for instance X-ray crystallographic analysis, depend on homogeneous preparations of proteins. The use of heterologous expression systems with bacteria as host cells is a well established methodology. Other host systems include yeast, insect cells and plant cells. The technology for cloning and expression of proteins, vectors with selectable markers, enhancers, trafficking signals and a range of facile protocols for over-expression are also readily available. However, often it is feasible to express only individual domains of large multi-domain proteins efficiently in heterologous systems. Even when the entire polypeptide can be expressed it is not always possible for the host cell to perform the necessary post-translational modifications. Furthermore, it is often difficult to obtain sufficient material— tissues/cells—to enable recovery of requisite quantities of the critical protein for physico-chemical analyses. If the source organism is easy to cultivate and adequate quantities of starting material can be acquired in a relatively short time, isolation and purification of the target protein(s) in the native state presents the best opportunity for insightful structural studies. On account of its rapid growth and simple nutrient requirements Neurospora is the ideal organism for acquisition of purified proteins. The following is a description of a procedure developed in my laboratory for isolation of highmolecular-mass stress-related Neurospora pr
{"title":"A procedure for parallel purification of four stress-related Neurospora proteins in their native state.","authors":"M. Kapoor","doi":"10.4148/1941-4765.1077","DOIUrl":"https://doi.org/10.4148/1941-4765.1077","url":null,"abstract":"A procedure is described for isolation and purification of four high-molecular mass stress-responsive proteins from the same starting material. This regular paper is available in Fungal Genetics Reports: https://newprairiepress.org/fgr/vol56/iss1/4 8 Fungal Genetics Reports A procedure for parallel purification of four stress-related Neurospora proteins in their native state. M. Kapoor. Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada Fungal Genetics Reports 65:8-11 A procedure is described for isolation and purification of four high-molecular mass stress-responsive proteins from the same starting material. Proteins are the major components determining cellular growth, metabolism, regulation, repair, homeostatic mechanisms, differentiation, organogenesis, response to environmental factors and ultimately survival. Extensive protein networks form the basis of interlocking metabolic pathways and their regulatory circuits in the eukaryotic and prokaryotic cells, involving transient interactions among a large, overwhelming array of actors. Availability of purified proteins in their native state is critical on account of the universal interest in unraveling how proteins function in their endogenous intracellular environment. With the rapid progress in genomics and availability of an ever increasing number of crystal structures, an understanding of the molecular basis of interactions of proteins with ligands, substrates and regulatory molecules is achievable. Structural studies, for instance X-ray crystallographic analysis, depend on homogeneous preparations of proteins. The use of heterologous expression systems with bacteria as host cells is a well established methodology. Other host systems include yeast, insect cells and plant cells. The technology for cloning and expression of proteins, vectors with selectable markers, enhancers, trafficking signals and a range of facile protocols for over-expression are also readily available. However, often it is feasible to express only individual domains of large multi-domain proteins efficiently in heterologous systems. Even when the entire polypeptide can be expressed it is not always possible for the host cell to perform the necessary post-translational modifications. Furthermore, it is often difficult to obtain sufficient material— tissues/cells—to enable recovery of requisite quantities of the critical protein for physico-chemical analyses. If the source organism is easy to cultivate and adequate quantities of starting material can be acquired in a relatively short time, isolation and purification of the target protein(s) in the native state presents the best opportunity for insightful structural studies. On account of its rapid growth and simple nutrient requirements Neurospora is the ideal organism for acquisition of purified proteins. The following is a description of a procedure developed in my laboratory for isolation of highmolecular-mass stress-related Neurospora pr","PeriodicalId":12490,"journal":{"name":"Fungal Genetics Reports","volume":"47 1","pages":"8-11"},"PeriodicalIF":0.0,"publicationDate":"2009-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80532266","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
This bibliography attempts to cover genetical and biochemical publications on Aspergillus nidulans and also includes selected references to related species and topics. Entries have been checked as far as possible, but please tell me of any errors and omissions. Authors are kindly requested to send a copy of each article to the FGSC for its reprint collection. This bibliography is available in Fungal Genetics Reports: https://newprairiepress.org/fgr/vol56/iss1/6 Aspergillus Bibliography 2009 This bibliography attempts to cover genetical and biochemical publications on Aspergillus nidulans and also includes selected references to related species and topics. Entries have been checked as far as possible, but please tell me of any errors and omissions. Authors are kindly requested to send a copy of each article to the FGSC for its reprint collection. John Clutterbuck. Faculty of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, UK. Email: j.clutterbuck@bio.gla.ac.uk Keyword or Author cross references 1. Abenza, J.F., Pantazopoulou, A., RodrÌguez, J.M., Galindo, A. & PeÒalva, M.A. 2009 Long-distance movement of Aspergillus nidulans early endosomes on microtubule tracks. Traffic. 10:57-75 2. Adachi, H., Tani, S., Kanamasa. S., Sumitani, J.-i. & Kawaguchi, T. 2009 Development of a homologous transformation system for Aspergillus acuelatus base on the sC gene encoding ATP-sulphurylase. Biosci. Biotechnol. Biochem. 73:1197-1199 3. Amaike, S. & Keller, N.P. 2009 Distinct roles for VeA and LeaA in development and pathogenesis of Aspergillus flavus. Eukaryot. Cell 8:1051-1060 4. Andersen, M.R. & Nielsen, J. 2009 Current status of systems biology in Aspergilli. Fungal Genet. Biol. 46 suppl.1:S180-S190 5. Apostolaki, A., Erpapazoglou, Z., Harispe, L., Billini, M., Kafasla, P., Kizis, D., PeÒalva, M.A., Scazzocchio, C. & Sophianopoulou, V. 2009 AgtA, the dicarboxylic amino acid transporter of Aspergillus nidulans, is concertedly down-regulated by exquisite sensitivity to nitrogen metabolite repression and ammonium-elicited endocytosis. Eukaryot. Cell 8:339-352 6. Ara·jo-Baz·n, L., Dhingra, S., Chu, J., Fern·ndez-Martinez, J., Calvo, A.M. & Espeso, E.A. 2009 Importin a is an essential nuclear import carrier adaptor required for proper sexual and asexual development and secondary metabolism in Aspergillus nidulans. Fungal Genet. Biol. 46:506-515 7. Bacha, N., Dao, H.P., Atoul, A., Mathieu, F., O’Callaghan, J., Puel, O., Liboz, T., Dobson, A.D.W. & Lebrihi, A. 2009 Cloning and characterization of novel methylsalicylic acid synthase gene involved in the biosynthesis of isoasperlactone and asperlactone in Aspergillus westerdijkiae. Fungal Genet. Biol. 46:742-749 8. Bahn, Y.-S. 2008 Master and commander in fungal pathogens: the two component system and the HOG signaling pathway. Eukaryot. Cell 7:2017-2036 9. Balajee, S.A. 2009 Aspergillus terreus complex. Med. Mycol. 47, suppl1:S42-6 10. Basheer, A., Berger, H., Reyes-Dominguez, Y., Gorfe
{"title":"Aspergillus Bibliography 2009","authors":"J. Clutterbuck","doi":"10.4148/1941-4765.1079","DOIUrl":"https://doi.org/10.4148/1941-4765.1079","url":null,"abstract":"This bibliography attempts to cover genetical and biochemical publications on Aspergillus nidulans and also includes selected references to related species and topics. Entries have been checked as far as possible, but please tell me of any errors and omissions. Authors are kindly requested to send a copy of each article to the FGSC for its reprint collection. This bibliography is available in Fungal Genetics Reports: https://newprairiepress.org/fgr/vol56/iss1/6 Aspergillus Bibliography 2009 This bibliography attempts to cover genetical and biochemical publications on Aspergillus nidulans and also includes selected references to related species and topics. Entries have been checked as far as possible, but please tell me of any errors and omissions. Authors are kindly requested to send a copy of each article to the FGSC for its reprint collection. John Clutterbuck. Faculty of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, UK. Email: j.clutterbuck@bio.gla.ac.uk Keyword or Author cross references 1. Abenza, J.F., Pantazopoulou, A., RodrÌguez, J.M., Galindo, A. & PeÒalva, M.A. 2009 Long-distance movement of Aspergillus nidulans early endosomes on microtubule tracks. Traffic. 10:57-75 2. Adachi, H., Tani, S., Kanamasa. S., Sumitani, J.-i. & Kawaguchi, T. 2009 Development of a homologous transformation system for Aspergillus acuelatus base on the sC gene encoding ATP-sulphurylase. Biosci. Biotechnol. Biochem. 73:1197-1199 3. Amaike, S. & Keller, N.P. 2009 Distinct roles for VeA and LeaA in development and pathogenesis of Aspergillus flavus. Eukaryot. Cell 8:1051-1060 4. Andersen, M.R. & Nielsen, J. 2009 Current status of systems biology in Aspergilli. Fungal Genet. Biol. 46 suppl.1:S180-S190 5. Apostolaki, A., Erpapazoglou, Z., Harispe, L., Billini, M., Kafasla, P., Kizis, D., PeÒalva, M.A., Scazzocchio, C. & Sophianopoulou, V. 2009 AgtA, the dicarboxylic amino acid transporter of Aspergillus nidulans, is concertedly down-regulated by exquisite sensitivity to nitrogen metabolite repression and ammonium-elicited endocytosis. Eukaryot. Cell 8:339-352 6. Ara·jo-Baz·n, L., Dhingra, S., Chu, J., Fern·ndez-Martinez, J., Calvo, A.M. & Espeso, E.A. 2009 Importin a is an essential nuclear import carrier adaptor required for proper sexual and asexual development and secondary metabolism in Aspergillus nidulans. Fungal Genet. Biol. 46:506-515 7. Bacha, N., Dao, H.P., Atoul, A., Mathieu, F., O’Callaghan, J., Puel, O., Liboz, T., Dobson, A.D.W. & Lebrihi, A. 2009 Cloning and characterization of novel methylsalicylic acid synthase gene involved in the biosynthesis of isoasperlactone and asperlactone in Aspergillus westerdijkiae. Fungal Genet. Biol. 46:742-749 8. Bahn, Y.-S. 2008 Master and commander in fungal pathogens: the two component system and the HOG signaling pathway. Eukaryot. Cell 7:2017-2036 9. Balajee, S.A. 2009 Aspergillus terreus complex. Med. Mycol. 47, suppl1:S42-6 10. Basheer, A., Berger, H., Reyes-Dominguez, Y., Gorfe","PeriodicalId":12490,"journal":{"name":"Fungal Genetics Reports","volume":"1 1","pages":"6"},"PeriodicalIF":0.0,"publicationDate":"2009-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75733316","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The Neurospora crassa temperature-sensitive mutant known as un-10 has been shown by a map-based complementation approach to be a single nucleotide change in the open reading frame of the eukaryotic translation initiation factor 3b (NCU02208.3). Authors Matthew Kinney, Aric Wiest, Michael Plamann, and Kevin McCluskey This regular paper is available in Fungal Genetics Reports: https://newprairiepress.org/fgr/vol56/iss1/3 6 Fungal Genetics Reports Identification of the Neurospora crassa mutation un-10 as a point mutation in a gene encoding eukaryotic translation initiation factor 3, subunit B. Matthew Kinney, Aric Wiest, Michael Plamann and Kevin McCluskey. Fungal Genetics Stock Center, School of Biological Sciences, University of Missouri-Kansas City Fungal Genetics Reports 56:6-7 The Neurospora crassa temperature-sensitive mutant known as un-10 has been shown by a map-based complementation approach to be a single nucleotide change in the open reading frame of the eukaryotic translation initiation factor 3b (NCU02208.3). ________________________________________________________________________ Inoue and Ishikawa defined a set of non-remediable, temperature-sensitive "unknown" mutants in Neurospora crassa (Inoue and Ishikawa,1970). To this day, the actual gene altered in many of these "unknown" mutants has not been determined. In order to add value to the Fungal Genetics Stock Center collection, we continue to define the genetic defects associated with these temperature-sensitive mutations (McCluskey et al., 2007, Wiest et al., 2008). Using a complementation-based approach, we have identified the mutation in un-10 as a missense mutation in the eIF3b open reading frame. Building on the demonstration by T. Schmidhauser, that cosmids from the pSV50 cosmid library (Vollmer and Yanofsky, 1986) complement the un-10 mutation in strain FGSC 2342 (Wilson, 1990), we had cosmids 10E12, 11D2, 16C5, and 23C1 end-sequenced. Based on this sequence data, the mutation in FGSC 2342 was predicted to be on contig 10 between bases 68,000 and 92,000 (Galagan, et al, 2003). We selected overlapping cosmids spanning this region and tested their ability to complement the un-10 mutation in FGSC 2342 using electroporation-based transformation (Margolin et. al, 2000; Table 1). Cosmid ID Colonies at 37oC (per ug DNA) Hyg Colonies at 24oC (per ug DNA) pLorist6xh 25D10 21 11 pLorist6xh 66B1 <1 7 pLorist6xh 75A9 56 18 pLorist6xh 107D10 24 7 pSV50 10E12 <1 ND pSV50 11D2 0 ND pSV50 23C1 0 ND No DNA 0 ND Table 1. Identification of cosmids that complement un-10 a. Not Done. The pSV50 does not encode hygromycin resistance. Complementation was successful with cosmids 25:D10, 75:A9 and 107:D10 but not 66:B1. There were four open reading frames in the region common to these overlapping cosmid clones: NCU02205.3, NCU02206.3, NCU02207.3 and NCU02208.3. We amplified copies of the genomic DNA for these open reading frames and used them to transform strain 2342 (Table 2). Only PCR product from N
基于图谱互补的方法显示，糙神经孢子虫的温度敏感突变体un-10是真核翻译起始因子3b (NCU02208.3)开放阅读框中的单个核苷酸变化。作者Matthew Kinney, Aric Wiest, Michael Plamann和Kevin McCluskey这篇常规论文可在真菌遗传学报告:https://newprairiepress.org/fgr/vol56/iss1/3 6真菌遗传学报告鉴定粗神经孢子虫突变un-10是编码真核翻译起始因子3亚基b的基因的点突变。Matthew Kinney, Aric Wiest, Michael Plamann和Kevin McCluskey。真菌遗传学报告56:6-7基于图谱互补的方法显示，草神经孢子虫的温度敏感突变体un-10在真核翻译启动因子3b (NCU02208.3)的开放阅读框中发生了单核苷酸变化。________________________________________________________________________ 井上和石川定义一组non-remediable,热敏“未知”突变体在粗糙脉孢菌(井上和石川,1970)。直到今天，在这些“未知的”突变体中，实际的基因改变还没有确定。为了增加真菌遗传库存中心收集的价值，我们继续定义与这些温度敏感突变相关的遗传缺陷(McCluskey et al.， 2007, Wiest et al.， 2008)。使用基于互补的方法，我们已经确定了un-10中的突变是eIF3b开放阅读框中的错义突变。基于T. Schmidhauser的论证，pSV50 cosmid文库中的cosmid (Vollmer和Yanofsky, 1986)与菌株FGSC 2342中的un10突变互补(Wilson, 1990)，我们对cosmid 10E12、11D2、16C5和23C1进行了末端测序。根据该序列数据，FGSC 2342的突变预计位于第10组68,000和92,000碱基之间(Galagan等，2003)。我们选择了跨越该区域的重叠cosmids，并使用基于电穿孔的转化测试了它们补充FGSC 2342中un-10突变的能力(Margolin等人，2000;表1)37℃时Cosmid菌落(每微克DNA) 24℃时Hyg菌落(每微克DNA) pLorist6xh 25D10 21 11 pLorist6xh 66B1 < 17 pLorist6xh 75a56 18 pLorist6xh 107D10 24 7 pSV50 10E12 <1 ND pSV50 11D2 0 ND pSV50 23C1 0 ND No DNA 0 ND识别与un- 10a互补的宇宙。尚未完成。pSV50不编码潮霉素抗性。与25:D10、75:A9和107:D10互补成功，但66:B1不成功。该区域共有4个开放阅读框:NCU02205.3、NCU02206.3、NCU02207.3和NCU02208.3。我们扩增了这些开放阅读框的基因组DNA拷贝，并用它们转化菌株2342(表2)。只有NCU02208.3的PCR产物补充了un-10突变。37℃时PCR产物菌落(每微克DNA) NCU02205 0 0 NCU02206 0 <1 NCU02207 0 <1 NCU02208 10 13 No DNA 0 0表2。从菌株2342的基因组DNA中直接获得的DNA序列显示，在1411位置有一个单T到C的转变，导致氨基酸残基471中色氨酸到精氨酸的变化。这种色氨酸残基在大多数真菌(图1)和更高级的真核生物中是保守的。酿酒酵母的同源基因PRT1具有赋予温度敏感表型的等位基因(Hanic-Joyce et al, 1987)。这些都不对应于突变1 Kinney等人:鉴定粗神经孢子虫突变un-10作为一个点，新草原出版社出版，2017
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This bibliography represents my attempt to collect all works dealing substantially with Neurospora. Please let me know of anything published in 2008 or 2009 that is not included here or in the previous bibliography, so that it might be mentioned next year. I would be especially happy to hear of chapters from books, and articles from journals not indexed in major bibliographic services. Please also let me know of any errors in citation. Please send reprints or copies of articles to the Fungal Genetics Stock Center. This bibliography is available in Fungal Genetics Reports: https://newprairiepress.org/fgr/vol56/iss1/5 2009 Neurospora Bibliography This bibliography represents my attempt to collect all works dealing substantially with Neurospora. Please let me know of anything published in 2008 or 2009 that is not included here or in the previous bibliography, so that it might be mentioned next year. I would be especially happy to hear of chapters from books, and articles from journals not indexed in major bibliographic services. Please also let me know of any errors in citation. Please send reprints or copies of articles to the Fungal Genetics Stock Center. Craig Wilson, 15236 Ashworth Ave. N., Shoreline WA 98133, USA (chwilso@gmail.com) Cross reference of author's names 1. Aanen, D.K., Debets, A.J.M., de Visser, J.A.G.M., and Hoekstra, R.F. 2008. The social evolution of somatic fusion. Bioessays 30:1193-1203. 2. Adhvaryu, K.K., and Selker, E.U. 2008. Protein phosphatase PP1 is required for normal DNA methylation in Neurospora. Genes Dev. 22:3391-3396. 3. Adio, S., and Woehlke, G. 2009. Properties of the Kinesin-3 NcKin3 motor domain and implications for neck function. FEBS J. 276:3641-3655. 4. Aiyar, R.S., Gagneur, J., and Steinmetz, L.M. 2008. Identification of mitochondrial disease genes through integrative analysis of multiple datasets. Methods 46:248-255. 5. Akman, O.E., Ciocchetta, F., Degasperi, A., and Guerriero, M.L. 2009. Modelling biological clocks with bio-pepa: stochasticity and robustness for the Neurospora crassa circadian network. Lect. Notes Bioinform. 5688:52-67. 6. Aldabbous, M. 2009. Isolation and characterization of Neurospora cell wall biosynthesis and anastomosisdefective mutants. Thesis (Ph.D.)--State University of New York at Buffalo, 176 p. 7. Aleman-Meza, B., Yu, Y.H., Schuttler, H.B., Arnold, J., and Taha, T.R. 2009. KINSOLVER: A simulator for computing large ensembles of biochemical and gene regulatory networks. Comput. Math. Appl. 57:420-435. 8. Aliyari, R., and Ding, S.W. 2009. RNA-based viral immunity initiated by the Dicer family of host immune receptors. Immunol. Rev. 227:176-188. 9. Allgaier, S., Taylor, R.D., Brudnaya, Y., Jacobson, D.J., Cambareri, E., and Stuart, W.D. 2009. Vaccine production in Neurospora crassa. Biologicals 37:128-132. 10. Allgaier, S., Weiland, N., Hamad, I., and Kempken, F. 2009. Expression of ribonuclease A and ribonuclease N(1) in the filamentous fungus Neurospora crassa. Appl. Microbiol.
{"title":"2009 Neurospora Bibliography","authors":"Craig Wilson","doi":"10.4148/1941-4765.1078","DOIUrl":"https://doi.org/10.4148/1941-4765.1078","url":null,"abstract":"This bibliography represents my attempt to collect all works dealing substantially with Neurospora. Please let me know of anything published in 2008 or 2009 that is not included here or in the previous bibliography, so that it might be mentioned next year. I would be especially happy to hear of chapters from books, and articles from journals not indexed in major bibliographic services. Please also let me know of any errors in citation. Please send reprints or copies of articles to the Fungal Genetics Stock Center. This bibliography is available in Fungal Genetics Reports: https://newprairiepress.org/fgr/vol56/iss1/5 2009 Neurospora Bibliography This bibliography represents my attempt to collect all works dealing substantially with Neurospora. Please let me know of anything published in 2008 or 2009 that is not included here or in the previous bibliography, so that it might be mentioned next year. I would be especially happy to hear of chapters from books, and articles from journals not indexed in major bibliographic services. Please also let me know of any errors in citation. Please send reprints or copies of articles to the Fungal Genetics Stock Center. Craig Wilson, 15236 Ashworth Ave. N., Shoreline WA 98133, USA (chwilso@gmail.com) Cross reference of author's names 1. Aanen, D.K., Debets, A.J.M., de Visser, J.A.G.M., and Hoekstra, R.F. 2008. The social evolution of somatic fusion. Bioessays 30:1193-1203. 2. Adhvaryu, K.K., and Selker, E.U. 2008. Protein phosphatase PP1 is required for normal DNA methylation in Neurospora. Genes Dev. 22:3391-3396. 3. Adio, S., and Woehlke, G. 2009. Properties of the Kinesin-3 NcKin3 motor domain and implications for neck function. FEBS J. 276:3641-3655. 4. Aiyar, R.S., Gagneur, J., and Steinmetz, L.M. 2008. Identification of mitochondrial disease genes through integrative analysis of multiple datasets. Methods 46:248-255. 5. Akman, O.E., Ciocchetta, F., Degasperi, A., and Guerriero, M.L. 2009. Modelling biological clocks with bio-pepa: stochasticity and robustness for the Neurospora crassa circadian network. Lect. Notes Bioinform. 5688:52-67. 6. Aldabbous, M. 2009. Isolation and characterization of Neurospora cell wall biosynthesis and anastomosisdefective mutants. Thesis (Ph.D.)--State University of New York at Buffalo, 176 p. 7. Aleman-Meza, B., Yu, Y.H., Schuttler, H.B., Arnold, J., and Taha, T.R. 2009. KINSOLVER: A simulator for computing large ensembles of biochemical and gene regulatory networks. Comput. Math. Appl. 57:420-435. 8. Aliyari, R., and Ding, S.W. 2009. RNA-based viral immunity initiated by the Dicer family of host immune receptors. Immunol. Rev. 227:176-188. 9. Allgaier, S., Taylor, R.D., Brudnaya, Y., Jacobson, D.J., Cambareri, E., and Stuart, W.D. 2009. Vaccine production in Neurospora crassa. Biologicals 37:128-132. 10. Allgaier, S., Weiland, N., Hamad, I., and Kempken, F. 2009. Expression of ribonuclease A and ribonuclease N(1) in the filamentous fungus Neurospora crassa. Appl. Microbiol. ","PeriodicalId":12490,"journal":{"name":"Fungal Genetics Reports","volume":"5 1","pages":"5"},"PeriodicalIF":0.0,"publicationDate":"2009-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76997612","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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