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Structures of the RNA polymerase- 54 reveal new and conserved regulatory strategies

DOI: 10.1126/science.aab1478 DOI Help
PMID: 26293966 PMID Help

Authors: Y. Yang (Imperial College London) , Vidya Darbari (Department of Life Sciences, Imperial College London, U.K.) , N. Zhang (Imperial College London) , Duo Lu (Imperial College London) , Robert Glyde (Imperial College London) , Y.-p. Wang (Peking University) , J. T. Winkelman (University of Wisconsin) , R. L. Gourse (University of Wisconsin) , K. S. Murakami (Pennsylvania State University) , M. Buck (Imperial College London) , Xiaodong Zhang (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Science , VOL 349 (6250) , PAGES 882 - 885

State: Published (Approved)
Published: August 2015
Diamond Proposal Number(s): 9424

Abstract: Transcription by RNA polymerase (RNAP) in bacteria requires specific promoter recognition by s factors. The major variant s factor (s54) initially forms a transcriptionally silent complex requiring specialized adenosine triphosphate–dependent activators for initiation. Our crystal structure of the 450-kilodalton RNAP-s54 holoenzyme at 3.8 angstroms reveals molecular details of s54 and its interactions with RNAP. The structure explains how s54 targets different regions in RNAP to exert its inhibitory function. Although s54 and the major s factor, s70, have similar functional domains and contact imilar regions of RNAP, unanticipated differences are observed in their domain arrangement and interactions with RNAP, explaining their distinct properties.Furthermore, we observe evolutionarily conserved regulatory hotspots in RNAPs that can be targeted by a diverse range of mechanisms to fine tune transcription.

Journal Keywords: X-Ray ; Enzyme; Evolution ; Molecular ; Gene; Holoenzymes ; Protein; Tertiary ; RNA; Transcription ; Genetic

Subject Areas: Medicine


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

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