Cell. 2012 Jul 20;150(2):291-303. doi: 10.1016/j.cell.2012.05.042.

An α helix to β barrel domain switch transforms the transcription factor RfaH into a translation factor.

Burmann BM, Knauer SH, Sevostyanova A, Schweimer K, Mooney RA, Landick R, Artsimovitch I, Rösch P.

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Lehrstuhl Biopolymere und Forschungszentrum für Bio-Makromoleküle, Universität Bayreuth, Universitätsstraße 30, 95447 Bayreuth, Germany.

Abstract

NusG homologs regulate transcription and coupled processes in all living organisms. The Escherichia coli (E. coli) two-domain paralogs NusG and RfaH have conformationally identical N-terminal domains (NTDs) but dramatically different carboxy-terminal domains (CTDs), a β barrel in NusG and an α hairpin in RfaH. Both NTDs interact with elongating RNA polymerase (RNAP) to reduce pausing. In NusG, NTD and CTD are completely independent, and NusG-CTD interacts with termination factor Rho or ribosomal protein S10. In contrast, RfaH-CTD makes extensive contacts with RfaH-NTD to mask an RNAP-binding site therein. Upon RfaH interaction with its DNA target, the operon polarity suppressor (ops) DNA, RfaH-CTD is released, allowing RfaH-NTD to bind to RNAP. Here, we show that the released RfaH-CTD completely refolds from an all-α to an all-β conformation identical to that of NusG-CTD. As a consequence, RfaH-CTD binding to S10 is enabled and translation of RfaH-controlled operons is strongly potentiated. PAPERFLICK:

Comment in

Unfolding the bridge between transcription and translation. [Cell. 2012]
Unfolding the bridge between transcription and translation.Svetlov V, Nudler E. Cell. 2012 Jul 20; 150(2):243-5.

PMID:: 22817892; [PubMed - indexed for MEDLINE]
PMCID:: PMC3430373; [Available on 2013/7/20]

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Structures reported by this article

Solution Structure Of Rfah Carboxyterminal Domain

PDB: 2LCL

Source: Escherichia coli O157:H7

Method: Solution Nmr

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