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
Biochemistryjournal_title
Biochemistryauthors
Bae SH,Liu D,Lim HM,Lee Y,Choi BSdoi
10.1021/bi701914tsubject
Has Abstractpub_date
2008-02-19 00:00:00pages
1993-2001issue
7eissn
0006-2960issn
1520-4995journal_volume
47pub_type
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