Structural basis for transcription initiation by bacterial ECF σ factors

Lingting Li, Chengli Fang, Ningning Zhuang, Tiantian Wang and Yu Zhang ()
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Lingting Li: Chinese Academy of Sciences
Chengli Fang: Chinese Academy of Sciences
Ningning Zhuang: Chinese Academy of Sciences
Tiantian Wang: Chinese Academy of Sciences
Yu Zhang: Chinese Academy of Sciences

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: Abstract Bacterial RNA polymerase employs extra-cytoplasmic function (ECF) σ factors to regulate context-specific gene expression programs. Despite being the most abundant and divergent σ factor class, the structural basis of ECF σ factor-mediated transcription initiation remains unknown. Here, we determine a crystal structure of Mycobacterium tuberculosis (Mtb) RNAP holoenzyme comprising an RNAP core enzyme and the ECF σ factor σH (σH-RNAP) at 2.7 Å, and solve another crystal structure of a transcription initiation complex of Mtb σH-RNAP (σH-RPo) comprising promoter DNA and an RNA primer at 2.8 Å. The two structures together reveal the interactions between σH and RNAP that are essential for σH-RNAP holoenzyme assembly as well as the interactions between σH-RNAP and promoter DNA responsible for stringent promoter recognition and for promoter unwinding. Our study establishes that ECF σ factors and primary σ factors employ distinct mechanisms for promoter recognition and for promoter unwinding.

Date: 2019
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DOI: 10.1038/s41467-019-09096-y

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