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  • Journal article
    Yang Y, Darbari VC, Zhang N, Lu D, Glyde R, Wang Y-P, Winkelman JT, Gourse RL, Murakami KS, Buck M, Zhang Xet al., 2015,

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

    , Science, Vol: 349, Pages: 882-885, ISSN: 0036-8075

    Transcription by RNA polymerase (RNAP) in bacteria requires specific promoter recognition by σ factors. The major variant σ factor (σ54) initially forms a transcriptionally silent complex requiring specialized adenosine triphosphate–dependent activators for initiation. Our crystal structure of the 450-kilodalton RNAP-σ54 holoenzyme at 3.8 angstroms reveals molecular details of σ54 and its interactions with RNAP. The structure explains how σ54 targets different regions in RNAP to exert its inhibitory function. Although σ54 and the major σ factor, σ70, have similar functional domains and contact similar 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 article
    Bush M, Ghosh T, Sawicka M, Moal IH, Bates PA, Dixon R, Zhang Xet al., 2015,

    The structural basis for enhancer-dependent assembly and activation of the AAA transcriptional activator NorR

    , MOLECULAR MICROBIOLOGY, Vol: 95, Pages: 17-30, ISSN: 0950-382X

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