N9L and L9N mutations toggle Hha binding and hemolysin regulation by Escherichia coli and Vibrio cholerae H-NS

被引:9
|
作者
Garcia, Jesus [1 ]
Madrid, Cristina [2 ]
Cendra, Mar [3 ]
Juarez, Antonio [2 ,3 ]
Pons, Miquel [1 ,4 ]
机构
[1] Inst Biomed Res, Barcelona 08028, Spain
[2] Univ Barcelona, Dept Microbiol, E-08028 Barcelona, Spain
[3] Inst Bioengn Catalunya, Barcelona 08028, Spain
[4] Univ Barcelona, Dept Organ Chem, E-08028 Barcelona, Spain
关键词
Nucleoid associated protein; H-NS; Hha; Transcription repression; NMR; Electrophoretic mobility shift assays; HISTONE-LIKE PROTEIN; ENTERICA SEROVAR TYPHIMURIUM; DIMERIZATION DOMAIN; GENE-EXPRESSION; DNA; SALMONELLA; OLIGOMERIZATION; ASSOCIATION; MECHANISM; MODULATOR;
D O I
10.1016/j.febslet.2009.07.054
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
Proteins of the Hha/YmoA family co-regulate with H-NS the expression of virulence factors in Enterobacteriaceae. Vibrio cholerae lacks Hha-like proteins and its H-NS (vcH-NS) is unable to bind Hha, in spite of the conservation of a key residue for Hha binding by Escherichia coli H-NS (ecH-NS). Exchange of the residues in position 9 between vcH-NS and ecH-NS strongly reduces Hha binding by ecH-NS and introduces it in vcH- NS. These mutations strongly affect the repression of the hemolysin operon in E. coli and the electrophoretic mobility of complexes formed with a DNA fragment containing its regulatory region. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2911 / 2916
页数:6
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