Structural basis of hypoxic gene regulation by the Rv0081 transcription factor of Mycobacteriumtuberculosis

FEBS Letters

article

Ashwani Kumar¹  Swastik Phulera¹  Arshad Rizvi²  Parshuram J. Sonawane¹  Hemendra S. Panwar¹  Sharmistha Banerjee²  Arvind Sahu¹  Shekhar C. Mande¹ 

[1] National Centre for Cell Science, SP Pune University Campus;Department of Biochemistry, University of Hyderabad

关键词: ArsR/SmtB family;    FHL regulator;    hypoxia protein;    phosphoserine;    Rv0081;   

DOI  :  10.1002/1873-3468.13375

来源: John Wiley & Sons Ltd.

【 摘 要 】

The HelD is a helicase-like protein binding to Bacillus subtilis RNA polymerase (RNAP), stimulating transcription in an ATP-dependent manner. Here, our small angle X-ray scattering data bring the first insights into the HelD structure: HelD is compact in shape and undergoes a conformational change upon substrate analog binding. Furthermore, the HelD domain structure is delineated, and a partial model of HelD is presented. In addition, the unique N-terminal domain of HelD is characterized as essential for its transcription-related function but not for ATPase activity, DNA binding, or binding to RNAP. The study provides a topological basis for further studies of the role of HelD in transcription.

【 授权许可】

Unknown