7khb
From Proteopedia
Escherichia coli RNA polymerase and rrnBP1 promoter open complex
Structural highlights
FunctionRPOA_ECOLI DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.[HAMAP-Rule:MF_00059] Publication Abstract from PubMedRibosomal RNA (rRNA) is most highly expressed in rapidly growing bacteria and is drastically downregulated under stress conditions by the global transcriptional regulator DksA and the alarmone ppGpp. Here, we determined cryo-electron microscopy structures of the Escherichia coli RNA polymerase (RNAP) sigma(70) holoenzyme during rRNA promoter recognition with and without DksA/ppGpp. RNAP contacts the UP element using dimerized alpha subunit carboxyl-terminal domains and scrunches the template DNA with the sigma finger and beta' lid to select the transcription start site favorable for rapid promoter escape. Promoter binding induces conformational change of sigma domain 2 that opens a gate for DNA loading and ejects sigma(1.1) from the RNAP cleft to facilitate open complex formation. DksA/ppGpp binding also opens the DNA loading gate, which is not coupled to sigma(1.1) ejection and impedes open complex formation. These results provide a molecular basis for the exceptionally active rRNA transcription and its vulnerability to DksA/ppGpp. Structural basis of ribosomal RNA transcription regulation.,Shin Y, Qayyum MZ, Pupov D, Esyunina D, Kulbachinskiy A, Murakami KS Nat Commun. 2021 Jan 22;12(1):528. doi: 10.1038/s41467-020-20776-y. PMID:33483500[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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