[No authors listed]
Bacterial RNA polymerase employs extra-cytoplasmic function (ECF) Ï factors to regulate context-specific gene expression programs. Despite being the most abundant and divergent Ï factor class, the structural basis of ECF Ï 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 Ï factor ÏH (ÏH-RNAP) at 2.7âà , and solve another crystal structure of a transcription initiation complex of Mtb ÏH-RNAP (ÏH-RPo) comprising promoter DNA and an RNA primer at 2.8âà . The two structures together reveal the interactions between ÏH and RNAP that are essential for ÏH-RNAP holoenzyme assembly as well as the interactions between ÏH-RNAP and promoter DNA responsible for stringent promoter recognition and for promoter unwinding. Our study establishes that ECF Ï factors and primary Ï factors employ distinct mechanisms for promoter recognition and for promoter unwinding.
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