海洋细菌木希旺氏菌厌氧电子传递链的丙烯酸酯还原酶

IF 2.3 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Yulia V. Bertsova, Marina V. Serebryakova, Vladimir A. Bogachev, Alexander A. Baykov, Alexander V. Bogachev
{"title":"海洋细菌木希旺氏菌厌氧电子传递链的丙烯酸酯还原酶","authors":"Yulia V. Bertsova, Marina V. Serebryakova, Vladimir A. Bogachev, Alexander A. Baykov, Alexander V. Bogachev","doi":"10.1134/s0006297924040096","DOIUrl":null,"url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>Many microorganisms are capable of anaerobic respiration in the absence of oxygen, by using different organic compounds as terminal acceptors in electron transport chain. We identify here an anaerobic respiratory chain protein responsible for acrylate reduction in the marine bacterium <i>Shewanella woodyi</i>. When the periplasmic proteins of <i>S. woodyi</i> were separated by ion exchange chromatography, acrylate reductase activity copurified with an ArdA protein (Swoo_0275). Heterologous expression of <i>S. woodyi</i> <i>ard</i>A gene (<i>swoo</i>_0275) in <i>Shewanella oneidensis</i> MR-1 cells did not result in the appearance in them of periplasmic acrylate reductase activity, but such activity was detected when the <i>ard</i>A gene was co-expressed with an <i>ard</i>B gene (<i>swoo</i>_0276). Together, these genes encode flavocytochrome <i>c</i> ArdAB, which is thus responsible for acrylate reduction in <i>S. woodyi</i> cells. ArdAB was highly specific for acrylate as substrate and reduced only methacrylate (at a 22-fold lower rate) among a series of other tested 2-enoates. In line with these findings, acrylate and methacrylate induced <i>ard</i>A gene expression in <i>S. woodyi</i> under anaerobic conditions, which was accompanied by the appearance of periplasmic acrylate reductase activity. ArdAB-linked acrylate reduction supports dimethylsulfoniopropionate-dependent anaerobic respiration in <i>S. woodyi</i> and, possibly, other marine bacteria.</p>","PeriodicalId":483,"journal":{"name":"Biochemistry (Moscow)","volume":null,"pages":null},"PeriodicalIF":2.3000,"publicationDate":"2024-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Acrylate Reductase of an Anaerobic Electron Transport Chain of the Marine Bacterium Shewanella woodyi\",\"authors\":\"Yulia V. Bertsova, Marina V. Serebryakova, Vladimir A. Bogachev, Alexander A. Baykov, Alexander V. Bogachev\",\"doi\":\"10.1134/s0006297924040096\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<h3 data-test=\\\"abstract-sub-heading\\\">Abstract</h3><p>Many microorganisms are capable of anaerobic respiration in the absence of oxygen, by using different organic compounds as terminal acceptors in electron transport chain. We identify here an anaerobic respiratory chain protein responsible for acrylate reduction in the marine bacterium <i>Shewanella woodyi</i>. When the periplasmic proteins of <i>S. woodyi</i> were separated by ion exchange chromatography, acrylate reductase activity copurified with an ArdA protein (Swoo_0275). Heterologous expression of <i>S. woodyi</i> <i>ard</i>A gene (<i>swoo</i>_0275) in <i>Shewanella oneidensis</i> MR-1 cells did not result in the appearance in them of periplasmic acrylate reductase activity, but such activity was detected when the <i>ard</i>A gene was co-expressed with an <i>ard</i>B gene (<i>swoo</i>_0276). Together, these genes encode flavocytochrome <i>c</i> ArdAB, which is thus responsible for acrylate reduction in <i>S. woodyi</i> cells. ArdAB was highly specific for acrylate as substrate and reduced only methacrylate (at a 22-fold lower rate) among a series of other tested 2-enoates. In line with these findings, acrylate and methacrylate induced <i>ard</i>A gene expression in <i>S. woodyi</i> under anaerobic conditions, which was accompanied by the appearance of periplasmic acrylate reductase activity. ArdAB-linked acrylate reduction supports dimethylsulfoniopropionate-dependent anaerobic respiration in <i>S. woodyi</i> and, possibly, other marine bacteria.</p>\",\"PeriodicalId\":483,\"journal\":{\"name\":\"Biochemistry (Moscow)\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2024-05-06\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemistry (Moscow)\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1134/s0006297924040096\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemistry (Moscow)","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1134/s0006297924040096","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

摘要 许多微生物能够在缺氧的情况下进行厌氧呼吸,它们在电子传递链中使用不同的有机化合物作为末端受体。我们在此发现了海洋细菌木质希瓦菌(Shewanella woodyi)中负责丙烯酸酯还原的厌氧呼吸链蛋白。用离子交换色谱法分离木质希沃菌的外质蛋白时,丙烯酸酯还原酶活性与 ArdA 蛋白(Swo_0275)共聚合。在 Shewanella oneidensis MR-1 细胞中异源表达 S. woodyi ardA 基因(swo_0275)不会导致细胞质周围出现丙烯酸酯还原酶活性,但当 ardA 基因与 ardB 基因(swo_0276)共同表达时,就能检测到丙烯酸酯还原酶活性。这些基因共同编码黄ocytochrome c ArdAB,因此它负责木质部S.细胞中的丙烯酸酯还原。ArdAB 对作为底物的丙烯酸酯具有高度特异性,在一系列测试的 2-烯酸盐中,它只还原甲基丙烯酸酯(还原率低 22 倍)。与这些发现相一致的是,在厌氧条件下,丙烯酸酯和甲基丙烯酸酯会诱导木质葡萄孢中的 ardA 基因表达,并伴随着丙烯酸酯还原酶外质活性的出现。与 ArdAB 链接的丙烯酸酯还原支持木化沙雷氏菌以及其他海洋细菌依赖二甲基硫代丙酸盐的厌氧呼吸。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Acrylate Reductase of an Anaerobic Electron Transport Chain of the Marine Bacterium Shewanella woodyi

Acrylate Reductase of an Anaerobic Electron Transport Chain of the Marine Bacterium Shewanella woodyi

Abstract

Many microorganisms are capable of anaerobic respiration in the absence of oxygen, by using different organic compounds as terminal acceptors in electron transport chain. We identify here an anaerobic respiratory chain protein responsible for acrylate reduction in the marine bacterium Shewanella woodyi. When the periplasmic proteins of S. woodyi were separated by ion exchange chromatography, acrylate reductase activity copurified with an ArdA protein (Swoo_0275). Heterologous expression of S. woodyi ardA gene (swoo_0275) in Shewanella oneidensis MR-1 cells did not result in the appearance in them of periplasmic acrylate reductase activity, but such activity was detected when the ardA gene was co-expressed with an ardB gene (swoo_0276). Together, these genes encode flavocytochrome c ArdAB, which is thus responsible for acrylate reduction in S. woodyi cells. ArdAB was highly specific for acrylate as substrate and reduced only methacrylate (at a 22-fold lower rate) among a series of other tested 2-enoates. In line with these findings, acrylate and methacrylate induced ardA gene expression in S. woodyi under anaerobic conditions, which was accompanied by the appearance of periplasmic acrylate reductase activity. ArdAB-linked acrylate reduction supports dimethylsulfoniopropionate-dependent anaerobic respiration in S. woodyi and, possibly, other marine bacteria.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Biochemistry (Moscow)
Biochemistry (Moscow) 生物-生化与分子生物学
CiteScore
4.70
自引率
3.60%
发文量
139
审稿时长
2 months
期刊介绍: Biochemistry (Moscow) is the journal that includes research papers in all fields of biochemistry as well as biochemical aspects of molecular biology, bioorganic chemistry, microbiology, immunology, physiology, and biomedical sciences. Coverage also extends to new experimental methods in biochemistry, theoretical contributions of biochemical importance, reviews of contemporary biochemical topics, and mini-reviews (News in Biochemistry).
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信