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脆弱拟杆菌金属β-内酰胺酶CcrA在大肠杆菌中的高水平表达需要dsbA或dsbB（编码周质二硫键催化系统一个组分的基因）发生突变。

A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coli.

作者信息

Alksne L E, Keeney D, Rasmussen B A

机构信息

Department of Molecular Biology, American Cyanamid Company, Pearl River, New York 10965.

出版信息

J Bacteriol. 1995 Jan;177(2):462-4. doi: 10.1128/jb.177.2.462-464.1995.

DOI:10.1128/jb.177.2.462-464.1995
PMID:7814337
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC176611/
Abstract

The metallo-beta-lactamase gene, ccrA, from Bacteroides fragilis is functionally expressed in Escherichia coli only in the presence of a genomic mutation in iarA or iarB (increased ampicillin resistance), identified in this study as dsbA or dsbB, respectively. DsbA and DsbB are components of a periplasmic protein disulfide bond-catalyzing system. Data indicated that DsbA interacted with CcrA, creating aberrant disulfide bond linkages that render CcrA proteolytically unstable. Mutations in dsbA or dsbB permissive for CcrA expression eliminated or greatly reduced DsbA activity, allowing CcrA to assume a disulfide bond-free and proteolytically stable conformation.

摘要

脆弱拟杆菌的金属β-内酰胺酶基因ccrA仅在iarA或iarB发生基因组突变（氨苄西林抗性增加）时才能在大肠杆菌中功能性表达，本研究分别确定为dsbA或dsbB。DsbA和DsbB是周质蛋白二硫键催化系统的组成部分。数据表明，DsbA与CcrA相互作用，形成异常的二硫键连接，使CcrA在蛋白水解方面不稳定。允许CcrA表达的dsbA或dsbB突变消除或大大降低了DsbA活性，使CcrA呈现无二硫键且蛋白水解稳定的构象。

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