Pub Date : 2024-04-01DOI: 10.1016/j.molp.2024.03.011
David R. Nelson, Alexandra Mystikou, Ashish Jaiswal, Cecilia Rad-Menéndez, Michael J. Preston, Frederik De Boever, Diana C. El Assal, Sarah Daakour, Michael W. Lomas, J. Twizere, David H. Green, W. Ratcliff, K. Salehi-Ashtiani
{"title":"Macroalgal deep genomics illuminate multiple paths to aquatic, photosynthetic multicellularity.","authors":"David R. Nelson, Alexandra Mystikou, Ashish Jaiswal, Cecilia Rad-Menéndez, Michael J. Preston, Frederik De Boever, Diana C. El Assal, Sarah Daakour, Michael W. Lomas, J. Twizere, David H. Green, W. Ratcliff, K. Salehi-Ashtiani","doi":"10.1016/j.molp.2024.03.011","DOIUrl":"https://doi.org/10.1016/j.molp.2024.03.011","url":null,"abstract":"","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":null,"pages":null},"PeriodicalIF":27.5,"publicationDate":"2024-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140780470","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-03-04Epub Date: 2024-01-17DOI: 10.1016/j.molp.2024.01.004
Amelia Henry
{"title":"A step forward in breeding for ratooning ability in rice.","authors":"Amelia Henry","doi":"10.1016/j.molp.2024.01.004","DOIUrl":"10.1016/j.molp.2024.01.004","url":null,"abstract":"","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":null,"pages":null},"PeriodicalIF":27.5,"publicationDate":"2024-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139491881","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ATP-binding cassette (ABC) transporters are integral membrane proteins that have evolved diverse functions fulfilled via the transport of various substrates. In Arabidopsis, the G subfamily of ABC proteins is particularly abundant and participates in multiple signaling pathways during plant development and stress responses. In this study, we revealed that two Arabidopsis ABCG transporters, ABCG16 and ABCG25, engage in ABA-mediated stress responses and early plant growth through endomembrane-specific dimerization-coupled transport of ABA and ABA-glucosyl ester (ABA-GE), respectively. We first revealed that ABCG16 contributes to osmotic stress tolerance via ABA signaling. More specifically, ABCG16 induces cellular ABA efflux in both yeast and plant cells. Using FRET analysis, we showed that ABCG16 forms obligatory homodimers for ABA export activity and that the plasma membrane-resident ABCG16 homodimers specifically respond to ABA, undergoing notable conformational changes. Furthermore, we demonstrated that ABCG16 heterodimerizes with ABCG25 at the endoplasmic reticulum (ER) membrane and facilitates the ER entry of ABA-GE in both Arabidopsis and tobacco cells. The specific responsiveness of the ABCG16-ABCG25 heterodimer to ABA-GE and the superior growth of their double mutant support an inhibitory role of these two ABCGs in early seedling establishment via regulation of ABA-GE translocation across the ER membrane. Our endomembrane-specific analysis of the FRET signals derived from the homo- or heterodimerized ABCG complexes allowed us to link endomembrane-biased dimerization to the translocation of distinct substrates by ABCG transporters, providing a prototypic framework for understanding the omnipotence of ABCG transporters in plant development and stress responses.
ATP 结合盒(ABC)转运体是通过转运各种底物而进化出的具有多种功能的整体膜蛋白。在拟南芥中,ABC 蛋白的 G 亚家族尤其丰富,它们参与了植物发育和胁迫响应过程中的多种信号通路。在这里,我们发现拟南芥的两个 ABCG 转运体 ABCG16 和 ABCG25 分别通过内膜特异性二聚化耦合转运 ABA 和 ABA-葡萄糖基酯(ABA-GE),参与 ABA 介导的胁迫响应和植物早期生长。我们首次发现ABCG16通过ABA信号转导促进了渗透胁迫耐受性。更具体地说,ABCG16 在酵母和植物细胞中都起到了刺激细胞 ABA 外流的作用。结合FRET(佛斯特共振能量转移)分析,我们发现ABCG16形成了ABA输出活性的强制性同源二聚体,并且质膜驻留的ABCG16同源二聚体对ABA有特异性反应,同源二聚体内部发生了显著的构象变化。此外,我们还证明 ABCG16 与 ABCG25 在 ER 膜上异源二聚体,促进了拟南芥和烟草细胞中 ABA-GE 进入 ER。ABCG16/ABCG25异源二聚体对ABA-GE的特异性反应以及双突变体jat1-2abcg25的优异生长证明了这两种ABCG通过调节ABA-GE在ER膜上的转运在早期幼苗形成过程中起到了抑制作用。我们对来自同源或异源二聚体 ABCG 复合物的 FRET 信号进行了内膜特异性分析,从而将偏重内膜的二聚化伙伴关系与 ABCG 转运体不同的底物转运联系起来,为理解 ABCG 转运体在植物发育和胁迫响应中的全能性提供了一个原型框架。
{"title":"Endomembrane-biased dimerization of ABCG16 and ABCG25 transporters determines their substrate selectivity in ABA-regulated plant growth and stress responses.","authors":"Yeling Zhou, Yuzhu Wang, Dong Zhang, Jiansheng Liang","doi":"10.1016/j.molp.2024.02.005","DOIUrl":"10.1016/j.molp.2024.02.005","url":null,"abstract":"<p><p>ATP-binding cassette (ABC) transporters are integral membrane proteins that have evolved diverse functions fulfilled via the transport of various substrates. In Arabidopsis, the G subfamily of ABC proteins is particularly abundant and participates in multiple signaling pathways during plant development and stress responses. In this study, we revealed that two Arabidopsis ABCG transporters, ABCG16 and ABCG25, engage in ABA-mediated stress responses and early plant growth through endomembrane-specific dimerization-coupled transport of ABA and ABA-glucosyl ester (ABA-GE), respectively. We first revealed that ABCG16 contributes to osmotic stress tolerance via ABA signaling. More specifically, ABCG16 induces cellular ABA efflux in both yeast and plant cells. Using FRET analysis, we showed that ABCG16 forms obligatory homodimers for ABA export activity and that the plasma membrane-resident ABCG16 homodimers specifically respond to ABA, undergoing notable conformational changes. Furthermore, we demonstrated that ABCG16 heterodimerizes with ABCG25 at the endoplasmic reticulum (ER) membrane and facilitates the ER entry of ABA-GE in both Arabidopsis and tobacco cells. The specific responsiveness of the ABCG16-ABCG25 heterodimer to ABA-GE and the superior growth of their double mutant support an inhibitory role of these two ABCGs in early seedling establishment via regulation of ABA-GE translocation across the ER membrane. Our endomembrane-specific analysis of the FRET signals derived from the homo- or heterodimerized ABCG complexes allowed us to link endomembrane-biased dimerization to the translocation of distinct substrates by ABCG transporters, providing a prototypic framework for understanding the omnipotence of ABCG transporters in plant development and stress responses.</p>","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":null,"pages":null},"PeriodicalIF":27.5,"publicationDate":"2024-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139702916","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-03-04Epub Date: 2024-01-19DOI: 10.1016/j.molp.2024.01.006
Paolo M Triozzi, Luca Brunello, Giacomo Novi, Gianmarco Ferri, Francesco Cardarelli, Elena Loreti, Mariano Perales, Pierdomenico Perata
Oxygen is essential for plant growth and development. Hypoxia occurs in plants due to limited oxygen availability following adverse environmental conditions as well in hypoxic niches in otherwise normoxic environments. However, the existence and functional integration of spatiotemporal oxygen dynamics with plant development remains unknown. In animal systems dynamic fluctuations in oxygen availability are known as cyclic hypoxia. In this study, we demonstrate that cyclic fluctuations in internal oxygen levels occur in young emerging leaves of Arabidopsis plants. Cyclic hypoxia in plants is based on a mechanism requiring the ETHYLENE RESPONSE FACTORS type VII (ERFVII) that are central components of the oxygen-sensing machinery in plants. The ERFVII-dependent mechanism allows precise adjustment of leaf growth in response to carbon status and oxygen availability within plant cells. This study thus establishes a functional connection between internal spatiotemporal oxygen dynamics and developmental processes of plants.
{"title":"Spatiotemporal oxygen dynamics in young leaves reveal cyclic hypoxia in plants.","authors":"Paolo M Triozzi, Luca Brunello, Giacomo Novi, Gianmarco Ferri, Francesco Cardarelli, Elena Loreti, Mariano Perales, Pierdomenico Perata","doi":"10.1016/j.molp.2024.01.006","DOIUrl":"10.1016/j.molp.2024.01.006","url":null,"abstract":"<p><p>Oxygen is essential for plant growth and development. Hypoxia occurs in plants due to limited oxygen availability following adverse environmental conditions as well in hypoxic niches in otherwise normoxic environments. However, the existence and functional integration of spatiotemporal oxygen dynamics with plant development remains unknown. In animal systems dynamic fluctuations in oxygen availability are known as cyclic hypoxia. In this study, we demonstrate that cyclic fluctuations in internal oxygen levels occur in young emerging leaves of Arabidopsis plants. Cyclic hypoxia in plants is based on a mechanism requiring the ETHYLENE RESPONSE FACTORS type VII (ERFVII) that are central components of the oxygen-sensing machinery in plants. The ERFVII-dependent mechanism allows precise adjustment of leaf growth in response to carbon status and oxygen availability within plant cells. This study thus establishes a functional connection between internal spatiotemporal oxygen dynamics and developmental processes of plants.</p>","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":null,"pages":null},"PeriodicalIF":27.5,"publicationDate":"2024-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139502669","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A new era for paclitaxel biosynthesis is coming.","authors":"Xiaonan Liu, Xiaoxi Zhu, Jian Cheng, Huifeng Jiang","doi":"10.1016/j.molp.2024.01.005","DOIUrl":"10.1016/j.molp.2024.01.005","url":null,"abstract":"","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":null,"pages":null},"PeriodicalIF":27.5,"publicationDate":"2024-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139502706","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-03-04Epub Date: 2024-02-10DOI: 10.1016/j.molp.2024.02.008
Claus Wasternack, Bettina Hause
{"title":"BFP1: One of 700 Arabidopsis F-box proteins mediates degradation of JA oxidases to promote plant immunity.","authors":"Claus Wasternack, Bettina Hause","doi":"10.1016/j.molp.2024.02.008","DOIUrl":"10.1016/j.molp.2024.02.008","url":null,"abstract":"","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":null,"pages":null},"PeriodicalIF":27.5,"publicationDate":"2024-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139716232","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-03-04Epub Date: 2024-02-08DOI: 10.1016/j.molp.2024.01.007
Jiangqin Wang, Yanping Luo, Fan Ye, Zhong Jie Ding, Shao Jian Zheng, Shuai Qiao, Yong Wang, Jiangtao Guo, Wei Yang, Nannan Su
Plant high-affinity K+ transporters (HKTs) mediate Na+ and K+ uptake, maintain Na+/K+ homeostasis, and therefore play crucial roles in plant salt tolerance. In this study, we present cryoelectron microscopy structures of HKTs from two classes, class I HKT1;1 from Arabidopsis thaliana (AtHKT1;1) and class II HKT2;1 from Triticum aestivum (TaHKT2;1), in both Na+- and K+-bound states at 2.6- to 3.0-Å resolutions. Both AtHKT1;1 and TaHKT2;1 function as homodimers. Each HKT subunit consists of four tandem domain units (D1-D4) with a repeated K+-channel-like M-P-M topology. In each subunit, D1-D4 assemble into an ion conduction pore with a pseudo-four-fold symmetry. Although both TaHKT2;1 and AtHKT1;1 have only one putative Na+ ion bound in the selectivity filter with a similar coordination pattern, the two HKTs display different K+ binding modes in the filter. TaHKT2;1 has three K+ ions bound in the selectivity filter, but AtHKT1;1 has only two K+ ions bound in the filter, which has a narrowed external entrance due to the presence of a Ser residue in the first filter motif. These structures, along with computational, mutational, and electrophysiological analyses, enable us to pinpoint key residues that are critical for the ion selectivity of HKTs. The findings provide new insights into the ion selectivity and ion transport mechanisms of plant HKTs and improve our understanding about how HKTs mediate plant salt tolerance and enhance crop growth.
{"title":"Structures and ion transport mechanisms of plant high-affinity potassium transporters.","authors":"Jiangqin Wang, Yanping Luo, Fan Ye, Zhong Jie Ding, Shao Jian Zheng, Shuai Qiao, Yong Wang, Jiangtao Guo, Wei Yang, Nannan Su","doi":"10.1016/j.molp.2024.01.007","DOIUrl":"10.1016/j.molp.2024.01.007","url":null,"abstract":"<p><p>Plant high-affinity K<sup>+</sup> transporters (HKTs) mediate Na<sup>+</sup> and K<sup>+</sup> uptake, maintain Na<sup>+</sup>/K<sup>+</sup> homeostasis, and therefore play crucial roles in plant salt tolerance. In this study, we present cryoelectron microscopy structures of HKTs from two classes, class I HKT1;1 from Arabidopsis thaliana (AtHKT1;1) and class II HKT2;1 from Triticum aestivum (TaHKT2;1), in both Na<sup>+</sup>- and K<sup>+</sup>-bound states at 2.6- to 3.0-Å resolutions. Both AtHKT1;1 and TaHKT2;1 function as homodimers. Each HKT subunit consists of four tandem domain units (D1-D4) with a repeated K<sup>+</sup>-channel-like M-P-M topology. In each subunit, D1-D4 assemble into an ion conduction pore with a pseudo-four-fold symmetry. Although both TaHKT2;1 and AtHKT1;1 have only one putative Na<sup>+</sup> ion bound in the selectivity filter with a similar coordination pattern, the two HKTs display different K<sup>+</sup> binding modes in the filter. TaHKT2;1 has three K<sup>+</sup> ions bound in the selectivity filter, but AtHKT1;1 has only two K<sup>+</sup> ions bound in the filter, which has a narrowed external entrance due to the presence of a Ser residue in the first filter motif. These structures, along with computational, mutational, and electrophysiological analyses, enable us to pinpoint key residues that are critical for the ion selectivity of HKTs. The findings provide new insights into the ion selectivity and ion transport mechanisms of plant HKTs and improve our understanding about how HKTs mediate plant salt tolerance and enhance crop growth.</p>","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":null,"pages":null},"PeriodicalIF":27.5,"publicationDate":"2024-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139712598","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}