1. Domain structure of HelD, an interaction partner of Bacillus subtilis RNA polymerase.
- Author
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Kovaľ T, Sudzinová P, Perháčová T, Trundová M, Skálová T, Fejfarová K, Šanderová H, Krásný L, Dušková J, and Dohnálek J
- Subjects
- Models, Molecular, Protein Binding, Protein Domains, Scattering, Small Angle, X-Ray Diffraction, Bacillus subtilis enzymology, Bacterial Proteins chemistry, Bacterial Proteins metabolism, DNA-Directed RNA Polymerases metabolism
- Abstract
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., (© 2019 Federation of European Biochemical Societies.)
- Published
- 2019
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