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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Amino Acid Residues in the GerAB Protein Important in the Function and Assembly of the Alanine Spore Germination Receptor of <named-content content-type="genus-species">Bacillus subtilis</named-content> 168<xref ref-type="fn" rid="FN2"><sup>▿</sup></xref></title><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="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">21378181</idno><idno type="pmc">3133103</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3133103</idno><idno type="RBID">PMC:3133103</idno><idno type="doi">10.1128/JB.01397-10</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000127</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000127</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Amino Acid Residues in the GerAB Protein Important in the Function and Assembly of the Alanine Spore Germination Receptor of <named-content content-type="genus-species">Bacillus subtilis</named-content> 168<xref ref-type="fn" rid="FN2"><sup>▿</sup></xref></title><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="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>The paradigm <italic>gerA</italic> operon is required for endospore germination in response to <sc>l</sc>-alanine as the sole germinant, and the three protein products, GerAA, GerAB, and GerAC are predicted to form a receptor complex in the spore inner membrane. GerAB shows homology to the amino acid-polyamine-organocation (APC) family of single-component transporters and is predicted to be an integral membrane protein with 10 membrane-spanning helices. Site-directed mutations were introduced into the <italic>gerAB</italic> gene at its natural location on the chromosome. Alterations to some charged or potential helix-breaking residues within membrane spans affected receptor function dramatically. In some cases, this is likely to reflect the complete loss of the GerA receptor complex, as judged by the absence of the germinant receptor protein GerAC, which suggests that the altered GerAB protein itself may be unstable or that the altered structure destabilizes the complex. Mutants that have a null phenotype for <sc>l</sc>-alanine germination but retain GerAC protein at near-normal levels are more likely to define amino acid residues of functional, rather than structural, importance. Single-amino-acid substitutions in each of the GerAB and GerAA proteins can prevent incorporation of GerAC protein into the spore; this provides strong evidence that the proteins within a specific receptor interact and that these interactions are required for receptor assembly. The lipoprotein nature of the GerAC receptor subunit is also important; an amino acid change in the prelipoprotein signal sequence in the <italic>gerAC1</italic> mutant results in the absence of GerAC protein from the spore.</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">21378181</article-id><article-id pub-id-type="pmc">3133103</article-id><article-id pub-id-type="publisher-id">1397-10</article-id><article-id pub-id-type="doi">10.1128/JB.01397-10</article-id><article-categories><subj-group subj-group-type="heading"><subject>Genetics and Molecular Biology</subject></subj-group></article-categories><title-group><article-title>Amino Acid Residues in the GerAB Protein Important in the Function and Assembly of the Alanine Spore Germination Receptor of <named-content content-type="genus-species">Bacillus subtilis</named-content> 168<xref ref-type="fn" rid="FN2"><sup>▿</sup></xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Cooper</surname><given-names>Gareth R.</given-names></name><xref ref-type="author-notes" rid="FN1">†</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: TMO Renewables Ltd., 40 Alan Turing Rd., Surrey Research Park, Guildford, Surrey GU2 7YF, 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>2261</fpage><lpage>2267</lpage><history><date date-type="received"><day>22</day><month>11</month><year>2010</year></date><date date-type="accepted"><day>17</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="zjb00911002261.pdf"></self-uri><abstract><p>The paradigm <italic>gerA</italic> operon is required for endospore germination in response to <sc>l</sc>-alanine as the sole germinant, and the three protein products, GerAA, GerAB, and GerAC are predicted to form a receptor complex in the spore inner membrane. GerAB shows homology to the amino acid-polyamine-organocation (APC) family of single-component transporters and is predicted to be an integral membrane protein with 10 membrane-spanning helices. Site-directed mutations were introduced into the <italic>gerAB</italic> gene at its natural location on the chromosome. Alterations to some charged or potential helix-breaking residues within membrane spans affected receptor function dramatically. In some cases, this is likely to reflect the complete loss of the GerA receptor complex, as judged by the absence of the germinant receptor protein GerAC, which suggests that the altered GerAB protein itself may be unstable or that the altered structure destabilizes the complex. Mutants that have a null phenotype for <sc>l</sc>-alanine germination but retain GerAC protein at near-normal levels are more likely to define amino acid residues of functional, rather than structural, importance. Single-amino-acid substitutions in each of the GerAB and GerAA proteins can prevent incorporation of GerAC protein into the spore; this provides strong evidence that the proteins within a specific receptor interact and that these interactions are required for receptor assembly. The lipoprotein nature of the GerAC receptor subunit is also important; an amino acid change in the prelipoprotein signal sequence in the <italic>gerAC1</italic> mutant results in the absence of GerAC protein from the spore.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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