Structure of the Nucleoid-Associated Protein Cnu Reveals Common Binding Sites for H-NS in Cnu and Hha

• Published in: Biochemistry (Easton) 2008-02, Vol.47 (7), p.1993-2001
• Main Authors: Bae, Sung-Hun, Liu, Dinan, Lim, Heon M., Lee, Younghoon, Choi, Byong-Seok
• Format: Article
• Language: English
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; Bacterial Proteins - metabolism; Binding Sites; Circular Dichroism; Cloning, Molecular; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; DNA-Binding Proteins - isolation & purification; DNA-Binding Proteins - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - metabolism; Models, Molecular; Protein Conformation; Protein Folding
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi701914t

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 α helices that are comparable with those of Hha, but it has significant flexibility in the C-terminal region and lacks a short α 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.