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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Effect of Amino Acid Substitutions in the GerAA Protein on the Function of the Alanine-Responsive Germinant Receptor of <named-content content-type="genus-species">Bacillus subtilis</named-content> Spores<xref ref-type="fn" rid="FN5"><sup>▿</sup></xref></title><author><name sortKey="Mongkolthanaruk, Wiyada" sort="Mongkolthanaruk, Wiyada" uniqKey="Mongkolthanaruk W" first="Wiyada" last="Mongkolthanaruk">Wiyada Mongkolthanaruk</name></author><author><name sortKey="Cooper, Gareth R" sort="Cooper, Gareth R" uniqKey="Cooper G" first="Gareth R." last="Cooper">Gareth R. Cooper</name></author><author><name sortKey="Mawer, Julia S P" sort="Mawer, Julia S P" uniqKey="Mawer J" first="Julia S. P." last="Mawer">Julia S. P. Mawer</name></author><author><name sortKey="Allan, Raymond N" sort="Allan, Raymond N" uniqKey="Allan R" first="Raymond N." last="Allan">Raymond N. Allan</name></author><author><name sortKey="Moir, Anne" sort="Moir, Anne" uniqKey="Moir A" first="Anne" last="Moir">Anne Moir</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">21378197</idno><idno type="pmc">3133101</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3133101</idno><idno type="RBID">PMC:3133101</idno><idno type="doi">10.1128/JB.01398-10</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000128</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000128</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Effect of Amino Acid Substitutions in the GerAA Protein on the Function of the Alanine-Responsive Germinant Receptor of <named-content content-type="genus-species">Bacillus subtilis</named-content> Spores<xref ref-type="fn" rid="FN5"><sup>▿</sup></xref></title><author><name sortKey="Mongkolthanaruk, Wiyada" sort="Mongkolthanaruk, Wiyada" uniqKey="Mongkolthanaruk W" first="Wiyada" last="Mongkolthanaruk">Wiyada Mongkolthanaruk</name></author><author><name sortKey="Cooper, Gareth R" sort="Cooper, Gareth R" uniqKey="Cooper G" first="Gareth R." last="Cooper">Gareth R. Cooper</name></author><author><name sortKey="Mawer, Julia S P" sort="Mawer, Julia S P" uniqKey="Mawer J" first="Julia S. P." last="Mawer">Julia S. P. Mawer</name></author><author><name sortKey="Allan, Raymond N" sort="Allan, Raymond N" uniqKey="Allan R" first="Raymond N." last="Allan">Raymond N. Allan</name></author><author><name sortKey="Moir, Anne" sort="Moir, Anne" uniqKey="Moir A" first="Anne" last="Moir">Anne Moir</name></author></analytic><series><title level="j">Journal of Bacteriology</title><idno type="ISSN">0021-9193</idno><idno type="eISSN">1098-5530</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Spores of <named-content content-type="genus-species">Bacillus subtilis</named-content> require the GerAA, GerAB, and GerAC receptor proteins for <sc>l</sc>-alanine-induced germination. Mutations in <italic>gerAA</italic>, both random and site directed, result in phenotypes that identify amino acid residues important for receptor function in broad terms. They highlight the functional importance of two regions in the central, integral membrane domain of GerAA. A P324S substitution in the first residue of a conserved PFPP motif results in a 10-fold increase in a spore's sensitivity to alanine; a P326S change results in the release of phase-dark spores, in which the receptor may be in an “activated” or “quasigerminated” state. Substitutions in residues 398 to 400, in a short loop between the last two likely membrane-spanning helices of this central domain, all affect the germination response, with the G398S substitution causing a temperature-sensitive defect. In others, there are wider effects on the receptor: if alanine is substituted for conserved residue N146, H304, or E330, a severe defect in <sc>l</sc>-alanine germination results. This correlates with the absence of GerAC, suggesting that the assembly or stability of the entire receptor complex has been compromised by the defect in GerAA. In contrast, severely germination-defective mutants such as E129K, L373F, S400F, and M409N mutants retain GerAC at normal levels, suggesting more local and specific effects on the function of GerAA itself. Further interpretation will depend on progress in structural analysis of the receptor proteins.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Bacteriol</journal-id><journal-id journal-id-type="hwp">jb</journal-id><journal-id journal-id-type="pmc">jb</journal-id><journal-id journal-id-type="publisher-id">JB</journal-id><journal-title-group><journal-title>Journal of Bacteriology</journal-title></journal-title-group><issn pub-type="ppub">0021-9193</issn><issn pub-type="epub">1098-5530</issn><publisher><publisher-name>American Society for Microbiology</publisher-name><publisher-loc>1752 N St., N.W., Washington, DC</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">21378197</article-id><article-id pub-id-type="pmc">3133101</article-id><article-id pub-id-type="publisher-id">1398-10</article-id><article-id pub-id-type="doi">10.1128/JB.01398-10</article-id><article-categories><subj-group subj-group-type="heading"><subject>Genetics and Molecular Biology</subject></subj-group></article-categories><title-group><article-title>Effect of Amino Acid Substitutions in the GerAA Protein on the Function of the Alanine-Responsive Germinant Receptor of <named-content content-type="genus-species">Bacillus subtilis</named-content> Spores<xref ref-type="fn" rid="FN5"><sup>▿</sup></xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Mongkolthanaruk</surname><given-names>Wiyada</given-names></name><xref ref-type="author-notes" rid="FN1">†</xref></contrib><contrib contrib-type="author"><name><surname>Cooper</surname><given-names>Gareth R.</given-names></name><xref ref-type="author-notes" rid="FN2">‡</xref></contrib><contrib contrib-type="author"><name><surname>Mawer</surname><given-names>Julia S. P.</given-names></name><xref ref-type="author-notes" rid="FN3">§</xref></contrib><contrib contrib-type="author"><name><surname>Allan</surname><given-names>Raymond N.</given-names></name><xref ref-type="author-notes" rid="FN4">¶</xref></contrib><contrib contrib-type="author"><name><surname>Moir</surname><given-names>Anne</given-names></name><xref ref-type="corresp" rid="cor1">*</xref></contrib><aff>Department of Molecular Biology & Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, United Kingdom</aff></contrib-group><author-notes><corresp id="cor1"><label>*</label>Corresponding author. Mailing address: <addr-line>Department of Molecular Biology & Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, United Kingdom</addr-line>. Phone: <phone>44 114 2224418</phone>. Fax: <fax>44 114 2491278</fax>. E-mail: <email>a.moir@sheffield.ac.uk</email>.</corresp><fn fn-type="present-address" id="FN1"><label>†</label><p>Present address: Department of Microbiology, Faculty of Science, Khon-Kaen University, Khon-Kaen 40002, Thailand.</p></fn><fn fn-type="present-address" id="FN2"><label>‡</label><p>Present address: TMO Renewables Ltd., 40 Alan Turing Rd., Surrey Research Park, Guildford, Surrey GU2 7YF, United Kingdom.</p></fn><fn fn-type="present-address" id="FN3"><label>§</label><p>Present address: Institute for Cell Biology, University of Edinburgh, Darwin Building, King's Buildings, Mayfield Road, Edinburgh EH9 3JR, United Kingdom.</p></fn><fn fn-type="present-address" id="FN4"><label>¶</label><p>Present address: School of Biological Sciences, University of Southampton, Highfield Campus, Southampton SO17 1BJ, United Kingdom.</p></fn></author-notes><pub-date pub-type="ppub"><month>5</month><year>2011</year></pub-date><volume>193</volume><issue>9</issue><fpage>2268</fpage><lpage>2275</lpage><history><date date-type="received"><day>22</day><month>11</month><year>2010</year></date><date date-type="accepted"><day>22</day><month>2</month><year>2011</year></date></history><permissions><copyright-statement>Copyright © 2011, American Society for Microbiology.</copyright-statement><copyright-year>2011</copyright-year><copyright-holder>American Society for Microbiology</copyright-holder></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zjb00911002268.pdf"></self-uri><abstract><p>Spores of <named-content content-type="genus-species">Bacillus subtilis</named-content> require the GerAA, GerAB, and GerAC receptor proteins for <sc>l</sc>-alanine-induced germination. Mutations in <italic>gerAA</italic>, both random and site directed, result in phenotypes that identify amino acid residues important for receptor function in broad terms. They highlight the functional importance of two regions in the central, integral membrane domain of GerAA. A P324S substitution in the first residue of a conserved PFPP motif results in a 10-fold increase in a spore's sensitivity to alanine; a P326S change results in the release of phase-dark spores, in which the receptor may be in an “activated” or “quasigerminated” state. Substitutions in residues 398 to 400, in a short loop between the last two likely membrane-spanning helices of this central domain, all affect the germination response, with the G398S substitution causing a temperature-sensitive defect. In others, there are wider effects on the receptor: if alanine is substituted for conserved residue N146, H304, or E330, a severe defect in <sc>l</sc>-alanine germination results. This correlates with the absence of GerAC, suggesting that the assembly or stability of the entire receptor complex has been compromised by the defect in GerAA. In contrast, severely germination-defective mutants such as E129K, L373F, S400F, and M409N mutants retain GerAC at normal levels, suggesting more local and specific effects on the function of GerAA itself. Further interpretation will depend on progress in structural analysis of the receptor proteins.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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