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在脆弱拟杆菌的金属β-内酰胺酶CcrA的两个半胱氨酸残基进行氨基酸替换后，其在大肠杆菌中呈现出对二硫键不敏感的表达。

Dsb-insensitive expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli after amino acid substitution at two cysteine residues within CcrA.

作者信息

Elksne L E, Rasmussen B A

机构信息

Discovery Research, Wyeth-Ayerst Research, Pearl River, New York 10965,USA.

出版信息

J Bacteriol. 1996 Jul;178(14):4306-9. doi: 10.1128/jb.178.14.4306-4309.1996.

DOI:10.1128/jb.178.14.4306-4309.1996
PMID:8763963
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC178192/
Abstract

It has previously been shown that functional expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli requires a mutation in either dsbA or dsbB, components of a periplasmic disulfide bond-catalyzing system. Site-directed mutagenesis resulting in the substitution of various amino acids for two of the three cysteine residues within CcrA allowed the expression of CcrA in a dsb+ background. This finding supports the hypothesis that DsbA creates aberrant disulfide bonds involving the Cys residues of CcrA.

摘要

先前的研究表明，脆弱拟杆菌的金属β-内酰胺酶CcrA在大肠杆菌中的功能性表达需要二硫键结合蛋白A（dsbA）或二硫键结合蛋白B（dsbB）发生突变，这两种蛋白是周质二硫键催化系统的组成部分。通过定点诱变，将CcrA中三个半胱氨酸残基中的两个替换为各种氨基酸，使得CcrA能够在dsb+背景下表达。这一发现支持了以下假设：DsbA会形成涉及CcrA半胱氨酸残基的异常二硫键。

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本文引用的文献

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A pathway for disulfide bond formation in vivo.体内二硫键形成的一条途径。
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An accuracy center in the ribosome conserved over 2 billion years.核糖体中的一个精确中心在超过20亿年的时间里一直保守存在。
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8
Contribution of enzymatic properties, cell permeability, and enzyme expression to microbiological activities of beta-lactams in three Bacteroides fragilis isolates that harbor a metallo-beta-lactamase gene.在三株携带金属β-内酰胺酶基因的脆弱拟杆菌分离株中，酶特性、细胞通透性和酶表达对β-内酰胺类抗生素微生物活性的贡献。
Antimicrob Agents Chemother. 1994 Sep;38(9):2116-20. doi: 10.1128/AAC.38.9.2116.
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Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo.大肠杆菌基因dsbB的鉴定与特性分析，该基因的产物参与体内二硫键的形成。
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Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.DsbC的结构与功能特性，一种参与大肠杆菌中二硫键形成的蛋白质。
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