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大肠杆菌B的dnaK基因以及携带温度敏感突变dnaK7(Ts)和dnaK756(Ts)的两个dnaK基因的DNA序列分析。

DNA sequence analysis of the dnaK gene of Escherichia coli B and of two dnaK genes carrying the temperature-sensitive mutations dnaK7(Ts) and dnaK756(Ts).

作者信息

Miyazaki T, Tanaka S, Fujita H, Itikawa H

机构信息

Department of Applied Microbiology, Nippon Roche Research Center, Kanagawa, Japan.

出版信息

J Bacteriol. 1992 Jun;174(11):3715-22. doi: 10.1128/jb.174.11.3715-3722.1992.

DOI:10.1128/jb.174.11.3715-3722.1992
PMID:1592823
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC206061/
Abstract

The DNA sequence of the dnaK gene of Escherichia coli was analyzed. The nucleotide sequence of the wild-type dnaK gene of E. coli B differed from that of E. coli K-12 in 15 bp, none of which altered the amino acid sequence. Two temperature-sensitive dnaK mutations were examined by cloning and sequence analyses. Results showed that one dnaK mutation, dnaK7(Ts), was a one-base substitution of T for C at nucleotide position 448 in the open reading frame yielding an amber nonsense codon. The other mutation, dnaK756(Ts), consisted of base substitutions (A for G) at three nucleotide positions, 95, 1364, and 1403, in the open reading frame resulting in an aspartic acid codon in place of a glycine codon.

摘要

对大肠杆菌dnaK基因的DNA序列进行了分析。大肠杆菌B野生型dnaK基因的核苷酸序列与大肠杆菌K-12的核苷酸序列在15个碱基对处存在差异,其中没有一个改变氨基酸序列。通过克隆和序列分析研究了两个温度敏感型dnaK突变。结果表明,一个dnaK突变体dnaK7(Ts)是开放阅读框中第448位核苷酸处的T被C单碱基取代,产生琥珀色无义密码子。另一个突变体dnaK756(Ts)由开放阅读框中三个核苷酸位置(95、1364和1403)的碱基取代(G被A取代)组成,导致甘氨酸密码子被天冬氨酸密码子取代。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/70b0/206061/99cc4af2c9f5/jbacter00077-0313-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/70b0/206061/f048229e4581/jbacter00077-0312-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/70b0/206061/99cc4af2c9f5/jbacter00077-0313-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/70b0/206061/f048229e4581/jbacter00077-0312-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/70b0/206061/99cc4af2c9f5/jbacter00077-0313-a.jpg

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引用本文的文献

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2
Partial loss of function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis.大肠杆菌中70 kDa热休克蛋白的同源物DnaK的功能部分丧失突变,影响与ATP结合和水解相关的高度保守氨基酸。
Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):7139-43. doi: 10.1073/pnas.89.15.7139.

本文引用的文献

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The genetics and regulation of heat-shock proteins.热休克蛋白的遗传学与调控
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