共 13 条
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.
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页码:2911 / 2916
页数:6
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