Domain structure of HelD, an interaction partner of Bacillus subtilis RNA polymerase

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 u...

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Bibliographic Details
Published in:FEBS letters 2019-05, Vol.593 (9), p.996-1005
Main Authors: Kovaľ, Tomáš, Sudzinová, Petra, Perháčová, Terézia, Trundová, Mária, Skálová, Tereza, Fejfarová, Karla, Šanderová, Hana, Krásný, Libor, Dušková, Jarmila, Dohnálek, Jan
Format: Article
Language:English
Subjects:
Bacillus subtilis
Bacillus subtilis - enzymology
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
DNA-Directed RNA Polymerases - metabolism
HelD
Models, Molecular
Protein Binding
Protein Domains
RNAP
SAXS
Scattering, Small Angle
X-Ray Diffraction
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.13385