Structures of the RNA polymerase-σ54 reveal new and conserved regulatory strategies

Yun Yang, Vidya C. Darbari, Nan Zhang, Duo Lu, Robert Glyde, Yi Ping Wang, Jared T. Winkelman, Richard L. Gourse, Katsuhiko S. Murakami, Martin Buck, Xiaodong Zhang

Research output: Contribution to journalArticlepeer-review

65 Scopus citations


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 s 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.

Original languageEnglish (US)
Pages (from-to)882-885
Number of pages4
Issue number6250
StatePublished - Aug 21 2015

All Science Journal Classification (ASJC) codes

  • General


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