Structural Insight into the Mechanism of σ32-Mediated Transcription Initiation of Bacterial RNA Polymerase.

ABSTRACT: Bacterial RNA polymerases (RNAP) form distinct holoenzymes with different σ factors to initiate diverse gene expression programs. In this study, we report a cryo-EM structure at 2.49 Å of RNA polymerase transcription complex containing a temperature-sensitive bacterial σ factor, σ³² (σ³²-RPo). The structure of σ³²-RPo reveals key interactions essential for the assembly of E. coli σ³²-RNAP holoenzyme and for promoter recognition and unwinding by σ³². Specifically, a weak interaction between σ³² and -35/-10 spacer is mediated by T128 and K130 in σ³². A histidine in σ³², rather than a tryptophan in σ⁷⁰, acts as a wedge to separate the base pair at the upstream junction of the transcriptio

SUBMITTER: Lu Q 

PROVIDER: S-EPMC10216364 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature