Domain structure of HelD, an interaction partner of Bacillus subtilis RNA polymerase
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- Keywords
- Bacillus subtilis, RNAP, SAXS, HelD,
- MeSH
- Bacillus subtilis enzymology MeSH
- Bacterial Proteins chemistry metabolism MeSH
- X-Ray Diffraction MeSH
- DNA-Directed RNA Polymerases metabolism MeSH
- Scattering, Small Angle MeSH
- Models, Molecular MeSH
- Protein Domains MeSH
- Protein Binding MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- DNA-Directed RNA Polymerases MeSH
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.
References provided by Crossref.org
Mycobacterial HelD connects RNA polymerase recycling with transcription initiation
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Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase
