Structure of the nucleoid-associated protein Cnu reveals common binding sites for H-NS in Cnu and Hha.

Abstract:

:Cnu is a nucleoid protein that has a high degree of sequence homology with Hha/YmoA family proteins, which bind to chromatin and regulate the expression of Escherichia coli virulence genes in response to changes in temperature or ionic strength. Here, we determined its solution structure and dynamic properties and mapped H-NS binding sites. Cnu consists of three alpha helices that are comparable with those of Hha, but it has significant flexibility in the C-terminal region and lacks a short alpha helix present in Hha. Upon increasing ionic strength, the helical structure of Cnu is destabilized, especially at the ends of the helices. The dominant H-NS binding sites, located at helix 3 as in Hha, reveal a common structural platform for H-NS binding. Our results may provide structural and dynamic bases for the similarity and dissimilarity between Cnu and Hha functions.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Bae SH,Liu D,Lim HM,Lee Y,Choi BS

doi

10.1021/bi701914t

subject

Has Abstract

pub_date

2008-02-19 00:00:00

pages

1993-2001

issue

7

eissn

0006-2960

issn

1520-4995

journal_volume

47

pub_type

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