The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain

The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain

<p>Abstract</p> <p>Background</p> <p>Cellular RNA polymerases (RNAPs) are complex molecular machines that combine catalysis with concerted conformational changes in the active center. Previous work showed that kinking of a hinge region near the C-terminus of the Bridge...

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Main Author: Weinzierl Robert OJ
Format: Article
Language:English
Published: BMC 2010-10-01
Series:BMC Biology
Online Access:http://www.biomedcentral.com/1741-7007/8/134
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spelling doaj-5db36940400a40c5bc2451b3f22027d22020-11-25T00:17:33ZengBMCBMC Biology1741-70072010-10-018113410.1186/1741-7007-8-134The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domainWeinzierl Robert OJ<p>Abstract</p> <p>Background</p> <p>Cellular RNA polymerases (RNAPs) are complex molecular machines that combine catalysis with concerted conformational changes in the active center. Previous work showed that kinking of a hinge region near the C-terminus of the Bridge Helix (BH-H<sub>C</sub>) plays a critical role in controlling the catalytic rate.</p> <p>Results</p> <p>Here, new evidence for the existence of an additional hinge region in the amino-terminal portion of the Bridge Helix domain (BH-H<sub>N</sub>) is presented. The nanomechanical properties of BH-H<sub>N </sub>emerge as a direct consequence of the highly conserved primary amino acid sequence. Mutations that are predicted to influence its flexibility cause corresponding changes in the rate of the nucleotide addition cycle (NAC). BH-H<sub>N </sub>displays functional properties that are distinct from BH-H<sub>C</sub>, suggesting that conformational changes in the Bridge Helix control the NAC via two independent mechanisms.</p> <p>Conclusions</p> <p>The properties of two distinct molecular hinges in the Bridge Helix of RNAP determine the functional contribution of this domain to key stages of the NAC by coordinating conformational changes in surrounding domains.</p> http://www.biomedcentral.com/1741-7007/8/134
collection DOAJ
language English
format Article
sources DOAJ
author Weinzierl Robert OJ
spellingShingle Weinzierl Robert OJ
The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain
BMC Biology
author_facet Weinzierl Robert OJ
author_sort Weinzierl Robert OJ
title The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain
title_short The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain
title_full The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain
title_fullStr The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain
title_full_unstemmed The nucleotide addition cycle of RNA polymerase is controlled by two molecular hinges in the Bridge Helix domain
title_sort nucleotide addition cycle of rna polymerase is controlled by two molecular hinges in the bridge helix domain
publisher BMC
series BMC Biology
issn 1741-7007
publishDate 2010-10-01
description <p>Abstract</p> <p>Background</p> <p>Cellular RNA polymerases (RNAPs) are complex molecular machines that combine catalysis with concerted conformational changes in the active center. Previous work showed that kinking of a hinge region near the C-terminus of the Bridge Helix (BH-H<sub>C</sub>) plays a critical role in controlling the catalytic rate.</p> <p>Results</p> <p>Here, new evidence for the existence of an additional hinge region in the amino-terminal portion of the Bridge Helix domain (BH-H<sub>N</sub>) is presented. The nanomechanical properties of BH-H<sub>N </sub>emerge as a direct consequence of the highly conserved primary amino acid sequence. Mutations that are predicted to influence its flexibility cause corresponding changes in the rate of the nucleotide addition cycle (NAC). BH-H<sub>N </sub>displays functional properties that are distinct from BH-H<sub>C</sub>, suggesting that conformational changes in the Bridge Helix control the NAC via two independent mechanisms.</p> <p>Conclusions</p> <p>The properties of two distinct molecular hinges in the Bridge Helix of RNAP determine the functional contribution of this domain to key stages of the NAC by coordinating conformational changes in surrounding domains.</p>
url http://www.biomedcentral.com/1741-7007/8/134
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AT weinzierlrobertoj nucleotideadditioncycleofrnapolymeraseiscontrolledbytwomolecularhingesinthebridgehelixdomain
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