{"title":"Disulfide Bond Formation in the Periplasm of <i>Escherichia coli</i>.","authors":"Bruno Manta, Dana Boyd, Mehmet Berkmen","doi":"10.1128/ecosalplus.ESP-0012-2018","DOIUrl":null,"url":null,"abstract":"<p><p>The formation of disulfide bonds is critical to the folding of many extracytoplasmic proteins in all domains of life. With the discovery in the early 1990s that disulfide bond formation is catalyzed by enzymes, the field of oxidative folding of proteins was born. <i>Escherichia coli</i> played a central role as a model organism for the elucidation of the disulfide bond-forming machinery. Since then, many of the enzymatic players and their mechanisms of forming, breaking, and shuffling disulfide bonds have become understood in greater detail. This article summarizes the discoveries of the past 3 decades, focusing on disulfide bond formation in the periplasm of the model prokaryotic host <i>E. coli</i>.</p>","PeriodicalId":11500,"journal":{"name":"EcoSal Plus","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2019-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11573287/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"EcoSal Plus","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1128/ecosalplus.ESP-0012-2018","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"Medicine","Score":null,"Total":0}
引用次数: 0
Abstract
The formation of disulfide bonds is critical to the folding of many extracytoplasmic proteins in all domains of life. With the discovery in the early 1990s that disulfide bond formation is catalyzed by enzymes, the field of oxidative folding of proteins was born. Escherichia coli played a central role as a model organism for the elucidation of the disulfide bond-forming machinery. Since then, many of the enzymatic players and their mechanisms of forming, breaking, and shuffling disulfide bonds have become understood in greater detail. This article summarizes the discoveries of the past 3 decades, focusing on disulfide bond formation in the periplasm of the model prokaryotic host E. coli.
EcoSal PlusImmunology and Microbiology-Microbiology
CiteScore
12.20
自引率
0.00%
发文量
4
期刊介绍：
EcoSal Plus is the authoritative online review journal that publishes an ever-growing body of expert reviews covering virtually all aspects of E. coli, Salmonella, and other members of the family Enterobacteriaceae and their use as model microbes for biological explorations. This journal is intended primarily for the research community as a comprehensive and continuously updated archive of the entire corpus of knowledge about the enteric bacterial cell. Thoughtful reviews focus on physiology, metabolism, genetics, pathogenesis, ecology, genomics, systems biology, and history E. coli and its relatives. These provide the integrated background needed for most microbiology investigations and are essential reading for research scientists. Articles contain links to E. coli K12 genes on the EcoCyc database site and are available as downloadable PDF files. Images and tables are downloadable to PowerPoint files.
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