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The ArcB leucine zipper domain is required for proper ArcB signaling
The Arc two-component system modulates the expression of numerous genes in response to respiratory growth conditions. This system comprises ArcA as the response regulator and ArcB as the sensor kinase. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-...
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Published in: | PloS one 2012-05, Vol.7 (5), p.e38187 |
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description | The Arc two-component system modulates the expression of numerous genes in response to respiratory growth conditions. This system comprises ArcA as the response regulator and ArcB as the sensor kinase. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation. Here, we report that the ArcB protein segment covering residues 70-121, fulfills the molecular characteristics of a leucine zipper containing coiled coil structure. Also, mutational analyses of this segment reveal three different phenotypical effects to be distributed along the coiled coil structure of ArcB, demonstrating that this motif is essential for proper ArcB signaling. |
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This system comprises ArcA as the response regulator and ArcB as the sensor kinase. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation. Here, we report that the ArcB protein segment covering residues 70-121, fulfills the molecular characteristics of a leucine zipper containing coiled coil structure. Also, mutational analyses of this segment reveal three different phenotypical effects to be distributed along the coiled coil structure of ArcB, demonstrating that this motif is essential for proper ArcB signaling.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0038187</identifier><identifier>PMID: 22666479</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Analysis ; ArcB protein ; Automation ; Biology ; Chemical bonds ; Coils ; Cysteine ; Cytosol ; DNA binding proteins ; E coli ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Gene expression ; Growth conditions ; Histidine ; Histidine kinase ; Kinases ; Laboratories ; Leucine ; Leucine zipper proteins ; Leucine Zippers ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Metabolism ; Metabolites ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Oxidation ; Phosphoric Monoester Hydrolases - metabolism ; Protein Kinases - chemistry ; Protein Kinases - genetics ; Protein Kinases - metabolism ; Proteins ; Residues ; Sensors ; Sequence Analysis ; Signaling ; Transmitters</subject><ispartof>PloS one, 2012-05, Vol.7 (5), p.e38187</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>2012 Nuñez Oreza et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Nuñez Oreza et al. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c789t-7a18469075a258d8efdc7ec2621f97887d6ce284ded8451bc0437cec65799a333</citedby><cites>FETCH-LOGICAL-c789t-7a18469075a258d8efdc7ec2621f97887d6ce284ded8451bc0437cec65799a333</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1325018102/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1325018102?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22666479$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Bravo, Alejandra</contributor><creatorcontrib>Nuñez Oreza, Luis Alberto</creatorcontrib><creatorcontrib>Alvarez, Adrián F</creatorcontrib><creatorcontrib>Arias-Olguín, Imilla I</creatorcontrib><creatorcontrib>Torres Larios, Alfredo</creatorcontrib><creatorcontrib>Georgellis, Dimitris</creatorcontrib><title>The ArcB leucine zipper domain is required for proper ArcB signaling</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The Arc two-component system modulates the expression of numerous genes in response to respiratory growth conditions. This system comprises ArcA as the response regulator and ArcB as the sensor kinase. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation. Here, we report that the ArcB protein segment covering residues 70-121, fulfills the molecular characteristics of a leucine zipper containing coiled coil structure. Also, mutational analyses of this segment reveal three different phenotypical effects to be distributed along the coiled coil structure of ArcB, demonstrating that this motif is essential for proper ArcB signaling.</description><subject>Amino Acid Sequence</subject><subject>Analysis</subject><subject>ArcB protein</subject><subject>Automation</subject><subject>Biology</subject><subject>Chemical bonds</subject><subject>Coils</subject><subject>Cysteine</subject><subject>Cytosol</subject><subject>DNA binding proteins</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Gene expression</subject><subject>Growth conditions</subject><subject>Histidine</subject><subject>Histidine kinase</subject><subject>Kinases</subject><subject>Laboratories</subject><subject>Leucine</subject><subject>Leucine zipper proteins</subject><subject>Leucine Zippers</subject><subject>Membrane Proteins - 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This system comprises ArcA as the response regulator and ArcB as the sensor kinase. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation. Here, we report that the ArcB protein segment covering residues 70-121, fulfills the molecular characteristics of a leucine zipper containing coiled coil structure. Also, mutational analyses of this segment reveal three different phenotypical effects to be distributed along the coiled coil structure of ArcB, demonstrating that this motif is essential for proper ArcB signaling.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22666479</pmid><doi>10.1371/journal.pone.0038187</doi><tpages>e38187</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Analysis ArcB protein Automation Biology Chemical bonds Coils Cysteine Cytosol DNA binding proteins E coli Escherichia coli Escherichia coli - enzymology Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Gene expression Growth conditions Histidine Histidine kinase Kinases Laboratories Leucine Leucine zipper proteins Leucine Zippers Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Metabolism Metabolites Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Mutation Oxidation Phosphoric Monoester Hydrolases - metabolism Protein Kinases - chemistry Protein Kinases - genetics Protein Kinases - metabolism Proteins Residues Sensors Sequence Analysis Signaling Transmitters |
title | The ArcB leucine zipper domain is required for proper ArcB signaling |
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