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Characterization of HelD, an interacting partner of RNA polymerase from Bacillus subtilis.


ABSTRACT: Bacterial RNA polymerase (RNAP) is an essential multisubunit protein complex required for gene expression. Here, we characterize YvgS (HelD) from Bacillus subtilis, a novel binding partner of RNAP. We show that HelD interacts with RNAP-core between the secondary channel of RNAP and the alpha subunits. Importantly, we demonstrate that HelD stimulates transcription in an ATP-dependent manner by enhancing transcriptional cycling and elongation. We demonstrate that the stimulatory effect of HelD can be amplified by a small subunit of RNAP, delta. In vivo, HelD is not essential but it is required for timely adaptations of the cell to changing environment. In summary, this study establishes HelD as a valid component of the bacterial transcription machinery.

SUBMITTER: Wiedermannova J 

PROVIDER: S-EPMC4005671 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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Characterization of HelD, an interacting partner of RNA polymerase from Bacillus subtilis.

Wiedermannová Jana J   Sudzinová Petra P   Kovaľ Tomaš T   Rabatinová Alžbeta A   Šanderova Hana H   Ramaniuk Olga O   Rittich Šimon Š   Dohnálek Jan J   Fu Zhihui Z   Halada Petr P   Lewis Peter P   Krásny Libor L  

Nucleic acids research 20140211 8


Bacterial RNA polymerase (RNAP) is an essential multisubunit protein complex required for gene expression. Here, we characterize YvgS (HelD) from Bacillus subtilis, a novel binding partner of RNAP. We show that HelD interacts with RNAP-core between the secondary channel of RNAP and the alpha subunits. Importantly, we demonstrate that HelD stimulates transcription in an ATP-dependent manner by enhancing transcriptional cycling and elongation. We demonstrate that the stimulatory effect of HelD can  ...[more]

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