2.50
Hdl Handle:
http://hdl.handle.net/10033/621008
Title:
RNA polymerase motions during promoter melting.
Authors:
Feklistov, Andrey; Bae, Brian; Hauver, Jesse; Lass-Napiorkowska, Agnieszka; Kalesse, Markus; Glaus, Florian; Altmann, Karl-Heinz; Heyduk, Tomasz; Landick, Robert; Darst, Seth A
Abstract:
All cellular RNA polymerases (RNAPs), from those of bacteria to those of man, possess a clamp that can open and close, and it has been assumed that the open RNAP separates promoter DNA strands and then closes to establish a tight grip on the DNA template. Here, we resolve successive motions of the initiating bacterial RNAP by studying real-time signatures of fluorescent reporters placed on RNAP and DNA in the presence of ligands locking the clamp in distinct conformations. We report evidence for an unexpected and obligatory step early in the initiation involving a transient clamp closure as a prerequisite for DNA melting. We also present a 2.6-angstrom crystal structure of a late-initiation intermediate harboring a rotationally unconstrained downstream DNA duplex within the open RNAP active site cleft. Our findings explain how RNAP thermal motions control the promoter search and drive DNA melting in the absence of external energy sources.
Affiliation:
Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
Citation:
RNA polymerase motions during promoter melting. 2017, 356 (6340):863-866 Science
Journal:
Science (New York, N.Y.)
Issue Date:
26-May-2017
URI:
http://hdl.handle.net/10033/621008
DOI:
10.1126/science.aam7858
PubMed ID:
28546214
Type:
Article
Language:
en
ISSN:
1095-9203
Appears in Collections:
publications of the department medicinal chemistry (MCH)

Full metadata record

DC FieldValue Language
dc.contributor.authorFeklistov, Andreyen
dc.contributor.authorBae, Brianen
dc.contributor.authorHauver, Jesseen
dc.contributor.authorLass-Napiorkowska, Agnieszkaen
dc.contributor.authorKalesse, Markusen
dc.contributor.authorGlaus, Florianen
dc.contributor.authorAltmann, Karl-Heinzen
dc.contributor.authorHeyduk, Tomaszen
dc.contributor.authorLandick, Roberten
dc.contributor.authorDarst, Seth Aen
dc.date.accessioned2017-07-11T14:46:33Z-
dc.date.available2017-07-11T14:46:33Z-
dc.date.issued2017-05-26-
dc.identifier.citationRNA polymerase motions during promoter melting. 2017, 356 (6340):863-866 Scienceen
dc.identifier.issn1095-9203-
dc.identifier.pmid28546214-
dc.identifier.doi10.1126/science.aam7858-
dc.identifier.urihttp://hdl.handle.net/10033/621008-
dc.description.abstractAll cellular RNA polymerases (RNAPs), from those of bacteria to those of man, possess a clamp that can open and close, and it has been assumed that the open RNAP separates promoter DNA strands and then closes to establish a tight grip on the DNA template. Here, we resolve successive motions of the initiating bacterial RNAP by studying real-time signatures of fluorescent reporters placed on RNAP and DNA in the presence of ligands locking the clamp in distinct conformations. We report evidence for an unexpected and obligatory step early in the initiation involving a transient clamp closure as a prerequisite for DNA melting. We also present a 2.6-angstrom crystal structure of a late-initiation intermediate harboring a rotationally unconstrained downstream DNA duplex within the open RNAP active site cleft. Our findings explain how RNAP thermal motions control the promoter search and drive DNA melting in the absence of external energy sources.en
dc.language.isoenen
dc.relationnfo:eu-repo/grantAgreement/EC/FP7/ 260872en
dc.rightsopenAccessen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleRNA polymerase motions during promoter melting.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.en
dc.identifier.journalScience (New York, N.Y.)en

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