Pub Date : 2002-01-01DOI: 10.1080/10425170290030051
I. Morlais, D. Severson
The complete sequence of the yellow fever mosquito, Aedes aegypti, mitochondrial cytochrome c oxidase subunit 1 gene has been identified. The nucleotide sequence codes for a 512 amino acid peptide. The AeCOI sequence is A+T rich (68.6%) and the codon usage is highly biased toward a preference for A- or T-ending triplets. The A. aegypti COI peptide shows high homology, up to 93% identity, with several other insect sequences and a phylogenetic analysis indicates that the A. aegypti sequence is closely related to two other mosquito species, Anopheles gambiae and A. quadrimaculatus. Comparisons of the nucleotide sequence for four A. aegypti laboratory strains revealed single nucleotide polymorphisms, with 25 nucleotide sites showing SNPs between strains. All SNPs occurred as synonymous transitions such that the peptide sequence is conserved among A. aegypti strains. RT-PCR analysis showed that COI is expressed at similar levels in all developmental stages and tissues.
{"title":"Complete Mitochondrial DNA Sequence and Amino Acid Analysis of the Cytochrome C Oxidase Subunit I ( COI ) from Aedes aegypti","authors":"I. Morlais, D. Severson","doi":"10.1080/10425170290030051","DOIUrl":"https://doi.org/10.1080/10425170290030051","url":null,"abstract":"The complete sequence of the yellow fever mosquito, Aedes aegypti, mitochondrial cytochrome c oxidase subunit 1 gene has been identified. The nucleotide sequence codes for a 512 amino acid peptide. The AeCOI sequence is A+T rich (68.6%) and the codon usage is highly biased toward a preference for A- or T-ending triplets. The A. aegypti COI peptide shows high homology, up to 93% identity, with several other insect sequences and a phylogenetic analysis indicates that the A. aegypti sequence is closely related to two other mosquito species, Anopheles gambiae and A. quadrimaculatus. Comparisons of the nucleotide sequence for four A. aegypti laboratory strains revealed single nucleotide polymorphisms, with 25 nucleotide sites showing SNPs between strains. All SNPs occurred as synonymous transitions such that the peptide sequence is conserved among A. aegypti strains. RT-PCR analysis showed that COI is expressed at similar levels in all developmental stages and tissues.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"32 1","pages":"123 - 127"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82824806","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}
Pub Date : 2002-01-01DOI: 10.1080/10425170290030015
S. Choudhuri, K. Ogura, C. Klaassen
The full-length coding sequence of rat liver specific organic anion transporter-1 (rlst-1/Oatp4/Slc21a10) was cloned by our group (Choudhuri et al., 2000) and by Cattori et al. (2000). We also cloned a splice variant of rlst-1 (Choudhuri et al., 2000). Another splice variant was cloned by Kakyo et al. (1999). We had also obtained a BAC clone from screening a BAC-Rat library, and determined the exon breakpoints to be able to determine the origin of the splice variants. Since our original publication, we have further characterized the rlst-1 gene. In this communication, we report the sequence of about 2.3 kb of the 50-flanking sequence of the rlst-1 gene that contains the promoter. We have mapped the transcription start site to define the precise location of the promoter. We also report here the splice junction sequence, and the partial sequences and lengths of introns of the rlst-1 gene. Finally, we have analyzed the codon usage bias in the rlst-1 coding sequence. Transcription start site was determined by capsite cloning as described by Choudhuri et al. (2001) with two major modifications. First, 20mg total RNA (instead of polyA mRNA) and secondly, Gene Racer RLM RACE system (In Vitrogen, CA), were used for this experiment. Sequence of the gene specific reverse primer (GSP), and nested gene specific reverse primer (nGSP) used, was as follows:
本研究组(Choudhuri et al.， 2000)和Cattori et al.(2000)分别克隆了大鼠肝脏特异性有机阴离子转运蛋白-1 (rlst-1/Oatp4/Slc21a10)全长编码序列。我们还克隆了rlst-1的一个剪接变体(Choudhuri et al.， 2000)。Kakyo等人(1999)克隆了另一个剪接变体。我们还通过筛选BAC- rat文库获得了一个BAC克隆，并确定了外显子断点，从而能够确定剪接变体的起源。自我们最初发表以来，我们进一步表征了rlst-1基因。在这篇文章中，我们报道了rlst-1基因50侧序列中含有启动子的约2.3 kb的序列。我们绘制了转录起始位点以确定启动子的精确位置。本文还报道了rlst-1基因的剪接连接序列、部分序列和内含子长度。最后，我们分析了rlst-1编码序列的密码子使用偏差。转录起始位点由Choudhuri等人(2001)描述的衣壳克隆确定，有两个主要的修改。首先，使用20mg总RNA(而不是polyA mRNA)，其次，使用Gene Racer RLM RACE系统(In Vitrogen, CA)进行实验。基因特异性反向引物(GSP)和巢式基因特异性反向引物(nGSP)的序列如下:
{"title":"Determination of Transcription Start Site and Analysis of Promoter Sequence, Splice Junction Sites, Intron Sequence and Codon Usage Bias of Rat Liver-specific Organic Anion Transporter-1 (rlst-1/Oatp-4/Slc21a10) Gene","authors":"S. Choudhuri, K. Ogura, C. Klaassen","doi":"10.1080/10425170290030015","DOIUrl":"https://doi.org/10.1080/10425170290030015","url":null,"abstract":"The full-length coding sequence of rat liver specific organic anion transporter-1 (rlst-1/Oatp4/Slc21a10) was cloned by our group (Choudhuri et al., 2000) and by Cattori et al. (2000). We also cloned a splice variant of rlst-1 (Choudhuri et al., 2000). Another splice variant was cloned by Kakyo et al. (1999). We had also obtained a BAC clone from screening a BAC-Rat library, and determined the exon breakpoints to be able to determine the origin of the splice variants. Since our original publication, we have further characterized the rlst-1 gene. In this communication, we report the sequence of about 2.3 kb of the 50-flanking sequence of the rlst-1 gene that contains the promoter. We have mapped the transcription start site to define the precise location of the promoter. We also report here the splice junction sequence, and the partial sequences and lengths of introns of the rlst-1 gene. Finally, we have analyzed the codon usage bias in the rlst-1 coding sequence. Transcription start site was determined by capsite cloning as described by Choudhuri et al. (2001) with two major modifications. First, 20mg total RNA (instead of polyA mRNA) and secondly, Gene Racer RLM RACE system (In Vitrogen, CA), were used for this experiment. Sequence of the gene specific reverse primer (GSP), and nested gene specific reverse primer (nGSP) used, was as follows:","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"1 1","pages":"103 - 107"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76129186","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}
Pub Date : 2002-01-01DOI: 10.1080/10425170290019900
A. Loukas, Alan P Brown, D. Pritchard
C-type lectins (C-TLs) are carbohydrate-binding proteins central to diverse physiological processes including immunity, venom-induced haemostasis and wound repair. Here we describe the cloning of Na - ctl -2, a cDNA encoding a secreted C-TL from the human hookworm Necator americanus. The transcript was detected in mRNA from adult worms but not infective larvae. The cDNA encoded an N-terminal secretory signal peptide followed by a long-form C-TL domain with sequence similarity to C-TL-like proteins from Caenorhabditis elegans and mammalian antigen presenting cell receptors, suggesting that hookworms might utilise this class of lectin to interrupt anti-parasite immune responses or interfere with host clotting mechanisms. This is the first report of a full-length cDNA encoding a lectin from hookworms. The unusually skewed representation of this protein family within different nematode genera and its subsequent impact on the evolution of nematode parasitism is discussed.
{"title":"Na - ctl -2, a cDNA Encoding a C-type Lectin Expressed Exclusively in Adult Necator americanus Hookworms","authors":"A. Loukas, Alan P Brown, D. Pritchard","doi":"10.1080/10425170290019900","DOIUrl":"https://doi.org/10.1080/10425170290019900","url":null,"abstract":"C-type lectins (C-TLs) are carbohydrate-binding proteins central to diverse physiological processes including immunity, venom-induced haemostasis and wound repair. Here we describe the cloning of Na - ctl -2, a cDNA encoding a secreted C-TL from the human hookworm Necator americanus. The transcript was detected in mRNA from adult worms but not infective larvae. The cDNA encoded an N-terminal secretory signal peptide followed by a long-form C-TL domain with sequence similarity to C-TL-like proteins from Caenorhabditis elegans and mammalian antigen presenting cell receptors, suggesting that hookworms might utilise this class of lectin to interrupt anti-parasite immune responses or interfere with host clotting mechanisms. This is the first report of a full-length cDNA encoding a lectin from hookworms. The unusually skewed representation of this protein family within different nematode genera and its subsequent impact on the evolution of nematode parasitism is discussed.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"42 1","pages":"61 - 65"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83900579","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}
Pub Date : 2002-01-01DOI: 10.1080/10425170290019865
M. Tokumoto, Y. Nagahama, T. Tokumoto
One of the eukaryotic polypeptide chain elongation factors, EF-1 g n i complex, is involved in polypeptide chain elongation via the GDP/GTP exchange activity of EF-1 f. In the complex, EF-1 n has been reported to be a major substrate for maturation promoting factor (MPF). Here, we present the cloning, sequencing and expression analysis of goldfish, Carassius auratus, EF-1 n from the goldfish ovary. The cloned cDNA was 1490 u bp in length and encoded 442 amino acids. The deduced amino acid sequence was highly homologous to EF-1 n from other species. Although, the phosphorylation site identified in Xenopus EF-1 n was not conserved in the goldfish homologue, phosphorylation analysis showed that the goldfish EF-1 n was phosphorylated by MPF. We concluded that EF-1 n is a substrate for MPF during oocyte maturation in goldfish.
真核生物多肽链延伸因子之一EF-1 g - n复合物通过EF-1 f的GDP/GTP交换活性参与多肽链延伸。在该复合物中，EF-1 n已被报道为成熟促进因子(MPF)的主要底物。本文报道了金鱼、鲫鱼、EF-1 n的克隆、测序和表达分析。克隆的cDNA全长1490 u bp，编码442个氨基酸。推导出的氨基酸序列与其他物种的EF-1 n高度同源。虽然在爪蟾EF-1 n中发现的磷酸化位点在金鱼同源物中并不保守，但磷酸化分析表明，金鱼EF-1 n被MPF磷酸化。我们认为EF-1 n是金鱼卵母细胞成熟过程中MPF的底物。
{"title":"A Major Substrate for MPF: cDNA Cloning and Expression of Polypeptide Chain Elongation Factor 1γ from Goldfish ( Carassius auratus )","authors":"M. Tokumoto, Y. Nagahama, T. Tokumoto","doi":"10.1080/10425170290019865","DOIUrl":"https://doi.org/10.1080/10425170290019865","url":null,"abstract":"One of the eukaryotic polypeptide chain elongation factors, EF-1 g n i complex, is involved in polypeptide chain elongation via the GDP/GTP exchange activity of EF-1 f. In the complex, EF-1 n has been reported to be a major substrate for maturation promoting factor (MPF). Here, we present the cloning, sequencing and expression analysis of goldfish, Carassius auratus, EF-1 n from the goldfish ovary. The cloned cDNA was 1490 u bp in length and encoded 442 amino acids. The deduced amino acid sequence was highly homologous to EF-1 n from other species. Although, the phosphorylation site identified in Xenopus EF-1 n was not conserved in the goldfish homologue, phosphorylation analysis showed that the goldfish EF-1 n was phosphorylated by MPF. We concluded that EF-1 n is a substrate for MPF during oocyte maturation in goldfish.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"1 1","pages":"27 - 31"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73937179","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}
Pub Date : 2002-01-01DOI: 10.1080/10425170290019856
M. Wolff, T. Su
During the last decade, molecular cloning has identified several families of multispecific organic ion transporters mediating the renal and hepatic elimination of organic ions. Clinically, these transporters play important roles in the renal tubular secretion and reabsorption of various drugs. They are also in part responsible for the drug pharmacologic responses, drug-drug interactions, and drug nephrotoxicity. This study describes 12 novel isoforms of the rat kidney organic anion transporter rOAT-K. These isoforms are spliced variants of the same gene arising from alternative splicing of six regions defined as A-F. The two previously reported isoforms rOAT-K1 and rOAT-K2 were also found to be spliced variants of this gene. The open reading frames of the 12 isoforms encode a range of 352-670 amino acid proteins. Tissue distribution studies showed that the majority of the isoforms are kidney- and liver-specific.
{"title":"Cloning and Tissue-specific Expression of Spliced Variants of the Rat Organic Anion Transporter (rOAT-K)","authors":"M. Wolff, T. Su","doi":"10.1080/10425170290019856","DOIUrl":"https://doi.org/10.1080/10425170290019856","url":null,"abstract":"During the last decade, molecular cloning has identified several families of multispecific organic ion transporters mediating the renal and hepatic elimination of organic ions. Clinically, these transporters play important roles in the renal tubular secretion and reabsorption of various drugs. They are also in part responsible for the drug pharmacologic responses, drug-drug interactions, and drug nephrotoxicity. This study describes 12 novel isoforms of the rat kidney organic anion transporter rOAT-K. These isoforms are spliced variants of the same gene arising from alternative splicing of six regions defined as A-F. The two previously reported isoforms rOAT-K1 and rOAT-K2 were also found to be spliced variants of this gene. The open reading frames of the 12 isoforms encode a range of 352-670 amino acid proteins. Tissue distribution studies showed that the majority of the isoforms are kidney- and liver-specific.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"16 1","pages":"15 - 25"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91288942","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}
Pub Date : 2002-01-01DOI: 10.1080/10425170290030033
GraceHu Yu, Jiang-ying Xu, Lin Xu, Kin-Sing Lee
Several mammalian thioredoxin cDNA sequences, namely that of human, macaca, ovine, bovine, equine and murine have been already registered in the Genbank database; but that of porcine is still not known. In this communication, we report the full-length cDNA sequence of porcine thioredoxin as determined by RT-PCR method. We also compared the protein sequence of thioredoxin from various mammals. Multialignment of the amino acid sequences between porcine and other mammalian species revealed that the sequences are highly conserved. Only one difference exists between the amino acid sequences of porcine and bovine thioredoxin.
{"title":"cDNA Sequence of Porcine Thioredoxin","authors":"GraceHu Yu, Jiang-ying Xu, Lin Xu, Kin-Sing Lee","doi":"10.1080/10425170290030033","DOIUrl":"https://doi.org/10.1080/10425170290030033","url":null,"abstract":"Several mammalian thioredoxin cDNA sequences, namely that of human, macaca, ovine, bovine, equine and murine have been already registered in the Genbank database; but that of porcine is still not known. In this communication, we report the full-length cDNA sequence of porcine thioredoxin as determined by RT-PCR method. We also compared the protein sequence of thioredoxin from various mammals. Multialignment of the amino acid sequences between porcine and other mammalian species revealed that the sequences are highly conserved. Only one difference exists between the amino acid sequences of porcine and bovine thioredoxin.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"3 1","pages":"113 - 115"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87982679","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}
Pub Date : 2001-01-01DOI: 10.3109/10425170109084457
D. Albouy, A. Castets, N. T. de Marsac
A gene cluster located downstream from gvpA in the cyanobacterium Pseudanabaena sp. strain PCC 6901 has been cloned and sequenced. The three genes, orfl, gvpN and gvpj, are consecutive with no intergenic region. In contrast to GvpN and Gvpj, which share high similarity at the amino acid level with their counterparts in other cyanobacteria and halophilic archaea, Orfl is only 29% identical to the C-terminal part of GvpC from Anabaena flos-aquae and its sequence organization is reminiscent of the halophilic archaeal GvpC.
{"title":"The Gas Vesicle Gene (gvp) Cluster of the Cyanobacterium Pseudanabaena sp. Strain PCC 6901","authors":"D. Albouy, A. Castets, N. T. de Marsac","doi":"10.3109/10425170109084457","DOIUrl":"https://doi.org/10.3109/10425170109084457","url":null,"abstract":"A gene cluster located downstream from gvpA in the cyanobacterium Pseudanabaena sp. strain PCC 6901 has been cloned and sequenced. The three genes, orfl, gvpN and gvpj, are consecutive with no intergenic region. In contrast to GvpN and Gvpj, which share high similarity at the amino acid level with their counterparts in other cyanobacteria and halophilic archaea, Orfl is only 29% identical to the C-terminal part of GvpC from Anabaena flos-aquae and its sequence organization is reminiscent of the halophilic archaeal GvpC.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"34 1","pages":"337 - 344"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78028141","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}
Pub Date : 2001-01-01DOI: 10.3109/10425170109084466
Jian Li, Yong Li, P. Brophy, D. Kershaw
Podocalyxin is a sialoglycoprotein of the glomerular podocytes, vascular endothelial cells, platelets, and hemopoietic stem cells. The function of podocalyxin is unknown, but it contains most of the protein bound sialic acid in the glomerulus and is considered vital in the structure and function of the glomerular filtration apparatus. The murine podocalyxin full-length cDNA has been determined and is 5318 base pairs. The gene localizes to chromosome 6B1 by FISH analysis and contains eight major exons with one additional alternatively spliced exon. The alternatively spliced isoform of podocalyxin codes for a truncated intracellular domain and is expressed in a tissue specific pattern in parallel with full-length podocalyxin. The organization of the gene structure of murine podocalyxin is similar to the murine CD34 gene and suggests a distant evolutionary relationship to CD34.
{"title":"Gene Structure and Alternative Splicing of Murine Podocalyxin: A member of the CD34 Sialomucin Family","authors":"Jian Li, Yong Li, P. Brophy, D. Kershaw","doi":"10.3109/10425170109084466","DOIUrl":"https://doi.org/10.3109/10425170109084466","url":null,"abstract":"Podocalyxin is a sialoglycoprotein of the glomerular podocytes, vascular endothelial cells, platelets, and hemopoietic stem cells. The function of podocalyxin is unknown, but it contains most of the protein bound sialic acid in the glomerulus and is considered vital in the structure and function of the glomerular filtration apparatus. The murine podocalyxin full-length cDNA has been determined and is 5318 base pairs. The gene localizes to chromosome 6B1 by FISH analysis and contains eight major exons with one additional alternatively spliced exon. The alternatively spliced isoform of podocalyxin codes for a truncated intracellular domain and is expressed in a tissue specific pattern in parallel with full-length podocalyxin. The organization of the gene structure of murine podocalyxin is similar to the murine CD34 gene and suggests a distant evolutionary relationship to CD34.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"56 1","pages":"407 - 412"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84923260","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}
Pub Date : 2001-01-01DOI: 10.3109/10425170109084474
Lori A. Preston, C. Bender, N. Schiller
Pseudomonas syringae produces alginate, an exopo-lysaccharide that contributes to the virulence and epiphytic fitness of this phytopathogenic bacterium. P. syringae also produces the aZgL-encoded alginate lyase, which cleaves the alginate biopolymer via a β-elimination reaction. The algL gene from P. syringae maps to a 1134 bp region within the alginate biosynthetic operon, and is similar to algL from Halomonas marina, P. aeruginosa, Azotobacter chroococcum, and A. vinelandii. algL from P. syringae was over expressed in Escherichia coli; two periplas-mic forms of AlgL were overproduced (40 and 37kDa). Both forms were enzymatically active and recognized by antibodies raised against AlgL from P. aeruginosa. Analysis of the regions flanking algL revealed significant homology to algX and algl, genes previously identified in the biosynthetic operon of other alginate-producing bacteria.
{"title":"Analysis and Expression of algL, which Encodes Alginate Lyase in Pseudomonas Syringae Pv. Syringae","authors":"Lori A. Preston, C. Bender, N. Schiller","doi":"10.3109/10425170109084474","DOIUrl":"https://doi.org/10.3109/10425170109084474","url":null,"abstract":"Pseudomonas syringae produces alginate, an exopo-lysaccharide that contributes to the virulence and epiphytic fitness of this phytopathogenic bacterium. P. syringae also produces the aZgL-encoded alginate lyase, which cleaves the alginate biopolymer via a β-elimination reaction. The algL gene from P. syringae maps to a 1134 bp region within the alginate biosynthetic operon, and is similar to algL from Halomonas marina, P. aeruginosa, Azotobacter chroococcum, and A. vinelandii. algL from P. syringae was over expressed in Escherichia coli; two periplas-mic forms of AlgL were overproduced (40 and 37kDa). Both forms were enzymatically active and recognized by antibodies raised against AlgL from P. aeruginosa. Analysis of the regions flanking algL revealed significant homology to algX and algl, genes previously identified in the biosynthetic operon of other alginate-producing bacteria.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"182 1","pages":"455 - 461"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80340978","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}
Pub Date : 2001-01-01DOI: 10.3109/10425170109084465
D. Jeoung, H. Kim
Ferritin serves as a storage protein for iron in animals. Complementary DNA encoding a heavy chain ferritin was cloned from the brain of Canis familiaris. The dog ferritin cDNA encodes a 182 amino acid that shows high levels of amino acid identity with vertebrate ferritins (90-98%). Near the cap region of the 5'-untranslated region, the dog H-ferritin mRNA displays a 28-nucleotide sequence that is exactly conserved in the corresponding region of the human and pig H-ferritin mRNA, thus making this sequence a prime candidate for involvement in the known translational regulation of H-ferritin by iron.
{"title":"Cloning and Sequence Analysis of cDNA for Heavy-chain Ferritin from the Canis familiaris","authors":"D. Jeoung, H. Kim","doi":"10.3109/10425170109084465","DOIUrl":"https://doi.org/10.3109/10425170109084465","url":null,"abstract":"Ferritin serves as a storage protein for iron in animals. Complementary DNA encoding a heavy chain ferritin was cloned from the brain of Canis familiaris. The dog ferritin cDNA encodes a 182 amino acid that shows high levels of amino acid identity with vertebrate ferritins (90-98%). Near the cap region of the 5'-untranslated region, the dog H-ferritin mRNA displays a 28-nucleotide sequence that is exactly conserved in the corresponding region of the human and pig H-ferritin mRNA, thus making this sequence a prime candidate for involvement in the known translational regulation of H-ferritin by iron.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"47 1","pages":"401 - 406"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82152050","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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