Structure of the Nucleoid-Associated Protein Cnu Reveals Common Binding Sites for H-NS in Cnu and Hha
详细信息 查看全文
- 作者：Sung-Hun Bae ; Dinan Liu ; Heon M. Lim ; Younghoon Lee ; Byong-Seok Choi
- 刊名：Biochemistry
- 出版年：2008
- 出版时间：February 19, 2008
- 年：2008
- 卷：47
- 期：7
- 页码：1993 - 2001
- 全文大小：424K
- 年卷期：v.47,no.7(February 19, 2008)
- ISSN：1520-4995
文摘
Cnu is a nucleoid protein that has a high degree of sequence homology with Hha/YmoA familyproteins, which bind to chromatin and regulate the expression of Escherichia coli virulence genes inresponse to changes in temperature or ionic strength. Here, we determined its solution structure and dynamicproperties and mapped H-NS binding sites. Cnu consists of three 
helices that are comparable withthose of Hha, but it has significant flexibility in the C-terminal region and lacks a short helix presentin Hha. Upon increasing ionic strength, the helical structure of Cnu is destabilized, especially at the endsof the helices. The dominant H-NS binding sites, located at helix 3 as in Hha, reveal a common structuralplatform for H-NS binding. Our results may provide structural and dynamic bases for the similarity anddissimilarity between Cnu and Hha functions.
helices that are comparable withthose of Hha, but it has significant flexibility in the C-terminal region and lacks a short helix presentin Hha. Upon increasing ionic strength, the helical structure of Cnu is destabilized, especially at the endsof the helices. The dominant H-NS binding sites, located at helix 3 as in Hha, reveal a common structuralplatform for H-NS binding. Our results may provide structural and dynamic bases for the similarity anddissimilarity between Cnu and Hha functions.