Burmann, B. M. and Knauer, S. H. and Sevostyanova, A. and Schweimer, K. and et al, . (2012) An α Helix to β Barrel Domain Switch Transforms the Transcription Factor RfaH into a Translation Factor. Cell, 150 (2). pp. 291-303.
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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.
| Item Type: | Article |
|---|---|
| Additional Information: | This project was supported by DFG (Ro617/18-1 to P.R.) and NIH (GM67153 to I.A.; GM38660 to R.L.). |
| Author Affiliation: | Lehrstuhl Biopolymere und Forschungszentrum fu¨ r Bio-Makromoleku¨ le, Universita¨ t Bayreuth, Universita¨ tsstraße 30 |
| Subjects: | Soil Science and Microbiology > Microbiology Plant Physiology and Biochemistry > Biochemistry |
| Divisions: | General |
| Depositing User: | Mr Siva Shankar |
| Date Deposited: | 20 Jul 2012 03:16 |
| Last Modified: | 20 Jul 2012 03:18 |
| Official URL: | http://dx.doi.org/10.1016/j.cell.2012.05.042 |
| URI: | http://eprints.icrisat.ac.in/id/eprint/6883 |
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