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Domain structure of HelD, an interaction partner of Bacillus subtilis RNA polymerase
T. Kovaľ, P. Sudzinová, T. Perháčová, M. Trundová, T. Skálová, K. Fejfarová, H. Šanderová, L. Krásný, J. Dušková, J. Dohnálek,
Language English Country Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Medline Complete (EBSCOhost)
from 2016-05-01 to 1 year ago
Wiley Free Content
from 1997 to 1 year ago
- 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
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
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- $a 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.
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