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Cryo-EM structure of sigma70 bound HK022 putRNA-associated E.coli RNA polymerase elongation complexCryo-EM structure of sigma70 bound HK022 putRNA-associated E.coli RNA polymerase elongation complex
Structural highlights
FunctionRPOB_ECOLI DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01321] Publication Abstract from PubMedTranscription, in which RNA polymerases (RNAPs) produce RNA from DNA, is the first step of gene expression. As such, it is highly regulated either by trans-elements like protein factors and/or by cis-elements like specific sequences on the DNA. Lambdoid phage HK022 contains a cis-element, put, which suppresses pausing and termination during transcription of the early phage genes. The putRNA transcript solely performs the anti-pausing/termination activities by interacting directly with the E.coli RNAP elongation complex (EC) by an unknown structural mechanism. In this study, we reconstituted putRNA-associated ECs and determined the structures using cryo-electron microscopy. The determined structures of putRNA-associated EC, putRNA-absent EC, and sigma(70)-bound EC suggest that the putRNA interaction with the EC counteracts swiveling, a conformational change previously identified to promote pausing and sigma(70) might modulate putRNA folding via sigma(70)-dependent pausing during elongation. Structural basis of transcriptional regulation by a nascent RNA element, HK022 putRNA.,Hwang S, Olinares PDB, Lee J, Kim J, Chait BT, King RA, Kang JY Nat Commun. 2022 Aug 15;13(1):4668. doi: 10.1038/s41467-022-32315-y. PMID:35970830[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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