All three J-domain proteins of the Escherichia coli DnaK chaperone machinery are DNA binding proteins

被引：15

作者：

Gur, E ^{[1
]}

Katz, C ^{[1
]}

Ron, EZ ^{[1
]}

机构：

[1] Tel Aviv Univ, George S Wise Fac Life Sci, Dept Mol Microbiol & Biotechnol, IL-69978 Tel Aviv, Israel

来源：

FEBS LETTERS | 2005年 / 579卷 / 09期

关键词：

heat shock response; DNA binding proteins; chaperones;

D O I：

10.1016/j.febslet.2005.01.084

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

DnaJ, DjIA and CbpA are the J-domain proteins of DnaK, the major Hsp70 of Escherichia coli. CbpA was originally discovered as a DNA binding protein. Here, we show that DNA binding is a property of DnaJ and DjIA as well. Of special interest in this respect is DjIA, as this cytoplasmic protein is membrane bound and, as shown here, its affinity for DNA is extremely high. The finding that all the three J-proteins of DnaK are DNA binding proteins sheds new light on the cellular activity of these proteins. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

收藏

页码：1935 / 1939

页数：5

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