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CryoEM structure of bacterial transcription close complex (RPc)CryoEM structure of bacterial transcription close complex (RPc)
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 PubMedGene transcription is carried out by RNA polymerase (RNAP) and requires the conversion of the initial closed promoter complex, where DNA is double stranded, to a transcription-competent open promoter complex, where DNA is opened up. In bacteria, RNAP relies on sigma factors for its promoter specificities. Using a special form of sigma factor (sigma(54)), which forms a stable closed complex and requires its activator that belongs to the AAA+ ATPases (ATPases associated with diverse cellular activities), we obtained cryo-electron microscopy structures of transcription initiation complexes that reveal a previously unidentified process of DNA melting opening. The sigma(54) amino terminus threads through the locally opened up DNA and then becomes enclosed by the AAA+ hexameric ring in the activator-bound intermediate complex. Our structures suggest how ATP hydrolysis by the AAA+ activator could remove the sigma(54) inhibition while helping to open up DNA, using sigma(54) amino-terminal peptide as a pry bar. Mechanisms of DNA opening revealed in AAA+ transcription complex structures.,Ye F, Gao F, Liu X, Buck M, Zhang X Sci Adv. 2022 Dec 21;8(51):eadd3479. doi: 10.1126/sciadv.add3479. Epub 2022 Dec , 21. PMID:36542713[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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