2mt4
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/NUSA_BACSU NUSA_BACSU]] Participates in both transcription termination and antitermination.[HAMAP-Rule:MF_00945] | [[http://www.uniprot.org/uniprot/NUSA_BACSU NUSA_BACSU]] Participates in both transcription termination and antitermination.[HAMAP-Rule:MF_00945] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pausing during transcription elongation is a fundamental activity in all kingdoms of life. In bacteria, the essential protein NusA modulates transcriptional pausing, but its mechanism of action has remained enigmatic. By combining structural and functional studies we show that a helical rearrangement induced in NusA upon interaction with RNA polymerase is the key to its modulatory function. This conformational change leads to an allosteric re-positioning of conserved basic residues that could enable their interaction with an RNA pause hairpin that forms in the exit channel of the polymerase. This weak interaction would stabilize the paused complex and increases the duration of the transcriptional pause. Allosteric spatial re-positioning of regulatory elements may represent a general approach used across all taxa for modulation of transcription and protein-RNA interactions. | ||
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| + | RNA polymerase-induced remodelling of NusA produces a pause enhancement complex.,Ma C, Mobli M, Yang X, Keller AN, King GF, Lewis PJ Nucleic Acids Res. 2015 Feb 17. pii: gkv108. PMID:25690895<ref>PMID:25690895</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:23, 4 March 2015
Solution structure of the N-terminal domain of NUSA from B. Subtilis
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