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Characterization of HelD, an interacting partner of RNA polymerase from Bacillus subtilis
J. Wiedermannová, P. Sudzinová, T. Kovaľ, A. Rabatinová, H. Šanderova, O. Ramaniuk, Š. Rittich, J. Dohnálek, Z. Fu, P. Halada, P. Lewis, L. Krásny,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Directory of Open Access Journals
od 2005
Free Medical Journals
od 1996
PubMed Central
od 1974
Europe PubMed Central
od 1974
Open Access Digital Library
od 1996-01-01 do 2030-12-31
Open Access Digital Library
od 1974-01-01
Open Access Digital Library
od 1996-01-01
Open Access Digital Library
od 1996-01-01
Medline Complete (EBSCOhost)
od 1996-01-01
Oxford Journals Open Access Collection
od 1996-01-01
ROAD: Directory of Open Access Scholarly Resources
od 1974
PubMed
24520113
DOI
10.1093/nar/gku113
Knihovny.cz E-zdroje
- MeSH
- adenosintrifosfát metabolismus MeSH
- Bacillus subtilis enzymologie genetika MeSH
- bakteriální proteiny izolace a purifikace metabolismus MeSH
- DNA řízené RNA-polymerasy chemie izolace a purifikace metabolismus MeSH
- DNA metabolismus MeSH
- elongace genetické transkripce MeSH
- fenotyp MeSH
- genetická transkripce * MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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.
Citace poskytuje Crossref.org
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- $a Wiedermannová, Jana $u Laboratory of Molecular Genetics of Bacteria, Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague 14220, Czech Republic, Department of Genetics and Microbiology, Faculty of Science, Charles University in Prague, Prague 12843, Czech Republic, Department of Structure Analysis of Biomacromolecules, Institute of Macromolecular Chemistry, Academy of Sciences of the Czech Republic, Prague 16206, Czech Republic, Laboratory of Structure and Function of Biomolecules, Institute of Biotechnology, Academy of Sciences of the Czech Republic, Prague 14220, Czech Republic, School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW 2308, Australia and Laboratory of Molecular Structure Characterization, Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague 14220, Czech Republic.
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- $a 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.
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