NDLI: The elongation factor RfaH and the initiation factor σ bind to the same site on the transcription elongation complex

Content Provider	PubMed Central
Author	Sevostyanova, Anastasiya Svetlov, Vladimir Vassylyev, Dmitry G. Irina, Artsimovitch
Copyright Year	2008
Abstract	RNA polymerase is a target for numerous regulatory events in all living cells. Recent studies identified a few “hot spots” on the surface of bacterial RNA polymerase that mediate its interactions with diverse accessory proteins. Prominent among these hot spots, the β′ subunit clamp helices serve as a major binding site for the initiation factor σ and for the elongation factor RfaH. Furthermore, the two proteins interact with the nontemplate DNA strand in transcription complexes and thus may interfere with each other's activity. We show that RfaH does not inhibit transcription initiation but, once recruited to RNA polymerase, abolishes σ-dependent pausing. We argue that this apparent competition is due to a steric exclusion of σ by RfaH that is stably bound to the nontemplate DNA and clamp helices, both of which are necessary for the σ recruitment to the transcription complex. Our findings highlight the key regulatory role played by the clamp helices during both initiation and elongation stages of transcription.
Related Links	http://dx.doi.org/10.1073/pnas.0708432105
Ending Page	870
Page Count	6
Starting Page	865
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	105
Language	English
Publisher	National Academy of Sciences
Publisher Date	2008-01-22
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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