Control of bacterial exoelectrogenesis by c-AMP-GMP
Identifieur interne : 000617 ( Ncbi/Merge ); précédent : 000616; suivant : 000618Control of bacterial exoelectrogenesis by c-AMP-GMP
Auteurs : James W. Nelson ; Narasimhan Sudarsan ; Grace E. Phillips ; Shira Stav ; Christina E. Lünse ; Phillip J. Mccown ; Ronald R. BreakerSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2015.
Abstract
The cyclic dinucleotides c-di-GMP and c-di-AMP are responsible for controlling broad changes in cell phenotypes during the life cycles of many bacterial species. To date, riboswitches that sense c-di-GMP and c-di-AMP have been discovered. The genomic locations of riboswitches reveal numerous genes that are controlled by these signaling compounds and thereby reveal the biological processes that are regulated. Herein, we report that a subset of conserved noncoding RNA domains previously annotated as c-di-GMP-I riboswitches in fact bind the newly discovered second messenger c-AMP-GMP. These riboswitches control many genes involved in the utilization of extracellular iron(III) oxide as an electron sink by various
Url:
DOI: 10.1073/pnas.1419264112
PubMed: 25848023
PubMed Central: 4418907
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Nelson</name><affiliation><nlm:aff id="aff1">Department of Chemistry,</nlm:aff></affiliation></author><author><name sortKey="Sudarsan, Narasimhan" sort="Sudarsan, Narasimhan" uniqKey="Sudarsan N" first="Narasimhan" last="Sudarsan">Narasimhan Sudarsan</name><affiliation><nlm:aff id="aff2">Department of Molecular, Cellular and Developmental Biology,</nlm:aff><wicri:noCountry code="subfield">Cellular and Developmental Biology</wicri:noCountry></affiliation><affiliation><nlm:aff id="aff3">Howard Hughes Medical Institute,<institution>Yale University</institution>, New Haven,<addr-line>CT</addr-line> 06520</nlm:aff></affiliation></author><author><name sortKey="Phillips, Grace E" sort="Phillips, Grace E" uniqKey="Phillips G" first="Grace E." last="Phillips">Grace E. 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Nelson</name><affiliation><nlm:aff id="aff1">Department of Chemistry,</nlm:aff></affiliation></author><author><name sortKey="Sudarsan, Narasimhan" sort="Sudarsan, Narasimhan" uniqKey="Sudarsan N" first="Narasimhan" last="Sudarsan">Narasimhan Sudarsan</name><affiliation><nlm:aff id="aff2">Department of Molecular, Cellular and Developmental Biology,</nlm:aff><wicri:noCountry code="subfield">Cellular and Developmental Biology</wicri:noCountry></affiliation><affiliation><nlm:aff id="aff3">Howard Hughes Medical Institute,<institution>Yale University</institution>, New Haven,<addr-line>CT</addr-line> 06520</nlm:aff></affiliation></author><author><name sortKey="Phillips, Grace E" sort="Phillips, Grace E" uniqKey="Phillips G" first="Grace E." last="Phillips">Grace E. Phillips</name><affiliation><nlm:aff id="aff4">Department of Molecular Biophysics and Biochemistry,</nlm:aff></affiliation></author><author><name sortKey="Stav, Shira" sort="Stav, Shira" uniqKey="Stav S" first="Shira" last="Stav">Shira Stav</name><affiliation><nlm:aff id="aff2">Department of Molecular, Cellular and Developmental Biology,</nlm:aff><wicri:noCountry code="subfield">Cellular and Developmental Biology</wicri:noCountry></affiliation></author><author><name sortKey="Lunse, Christina E" sort="Lunse, Christina E" uniqKey="Lunse C" first="Christina E." last="Lünse">Christina E. Lünse</name><affiliation><nlm:aff id="aff2">Department of Molecular, Cellular and Developmental Biology,</nlm:aff><wicri:noCountry code="subfield">Cellular and Developmental Biology</wicri:noCountry></affiliation></author><author><name sortKey="Mccown, Phillip J" sort="Mccown, Phillip J" uniqKey="Mccown P" first="Phillip J." last="Mccown">Phillip J. Mccown</name><affiliation><nlm:aff id="aff2">Department of Molecular, Cellular and Developmental Biology,</nlm:aff><wicri:noCountry code="subfield">Cellular and Developmental Biology</wicri:noCountry></affiliation></author><author><name sortKey="Breaker, Ronald R" sort="Breaker, Ronald R" uniqKey="Breaker R" first="Ronald R." last="Breaker">Ronald R. Breaker</name><affiliation><nlm:aff id="aff2">Department of Molecular, Cellular and Developmental Biology,</nlm:aff><wicri:noCountry code="subfield">Cellular and Developmental Biology</wicri:noCountry></affiliation><affiliation><nlm:aff id="aff3">Howard Hughes Medical Institute,<institution>Yale University</institution>, New Haven,<addr-line>CT</addr-line> 06520</nlm:aff></affiliation><affiliation><nlm:aff id="aff4">Department of Molecular Biophysics and Biochemistry,</nlm:aff></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Significance</title><p>The cyclic dinucleotides c-di-GMP and c-di-AMP are responsible for controlling broad changes in cell phenotypes during the life cycles of many bacterial species. To date, riboswitches that sense c-di-GMP and c-di-AMP have been discovered. The genomic locations of riboswitches reveal numerous genes that are controlled by these signaling compounds and thereby reveal the biological processes that are regulated. Herein, we report that a subset of conserved noncoding RNA domains previously annotated as c-di-GMP-I riboswitches in fact bind the newly discovered second messenger c-AMP-GMP. These riboswitches control many genes involved in the utilization of extracellular iron(III) oxide as an electron sink by various <italic>Geobacter</italic> species. Our findings reveal additional roles for this recently discovered signaling molecule.</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">Proc Natl Acad Sci U S A</journal-id><journal-id journal-id-type="iso-abbrev">Proc. Natl. Acad. Sci. U.S.A</journal-id><journal-id journal-id-type="hwp">pnas</journal-id><journal-id journal-id-type="pmc">pnas</journal-id><journal-id journal-id-type="publisher-id">PNAS</journal-id><journal-title-group><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title></journal-title-group><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn><publisher><publisher-name>National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25848023</article-id><article-id pub-id-type="pmc">4418907</article-id><article-id pub-id-type="publisher-id">201419264</article-id><article-id pub-id-type="doi">10.1073/pnas.1419264112</article-id><article-categories><subj-group subj-group-type="heading"><subject>Biological Sciences</subject><subj-group><subject>Biochemistry</subject></subj-group></subj-group></article-categories><title-group><article-title>Control of bacterial exoelectrogenesis by c-AMP-GMP</article-title><alt-title alt-title-type="short">c-AMP-GMP riboswitches</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Nelson</surname><given-names>James W.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="author-notes" rid="fn1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Sudarsan</surname><given-names>Narasimhan</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="aff" rid="aff3"><sup>c</sup></xref><xref ref-type="author-notes" rid="fn1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Phillips</surname><given-names>Grace E.</given-names></name><xref ref-type="aff" rid="aff4"><sup>d</sup></xref></contrib><contrib contrib-type="author"><name><surname>Stav</surname><given-names>Shira</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Lünse</surname><given-names>Christina E.</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>McCown</surname><given-names>Phillip J.</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="fn2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Breaker</surname><given-names>Ronald R.</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="aff" rid="aff3"><sup>c</sup></xref><xref ref-type="aff" rid="aff4"><sup>d</sup></xref><xref ref-type="corresp" rid="cor1"><sup>3</sup></xref></contrib><aff id="aff1"><sup>a</sup>Department of Chemistry,</aff><aff id="aff2"><sup>b</sup>Department of Molecular, Cellular and Developmental Biology,</aff><aff id="aff4"><sup>d</sup>Department of Molecular Biophysics and Biochemistry,</aff><aff id="aff3"><sup>c</sup>Howard Hughes Medical Institute,<institution>Yale University</institution>, New Haven,<addr-line>CT</addr-line> 06520</aff></contrib-group><author-notes><corresp id="cor1"><sup>3</sup>To whom correspondence should be addressed. Email: <email>ronald.breaker@yale.edu</email>.</corresp><fn fn-type="edited-by"><p>Edited by Gisela Storz, National Institutes of Health, Bethesda, MD, and approved March 8, 2015 (received for review October 6, 2014)</p></fn><fn fn-type="con"><p>Author contributions: J.W.N., N.S., and R.R.B. designed research; J.W.N., N.S., G.E.P., S.S., C.E.L., and P.J.M. performed research; J.W.N., N.S., C.E.L., and R.R.B. analyzed data; and J.W.N. and R.R.B. wrote the paper.</p></fn><fn fn-type="present-address" id="fn2"><p><sup>2</sup>Present address: Howard Hughes Medical Institute, Indiana University, Bloomington, IN 47405.</p></fn><fn fn-type="equal" id="fn1"><p><sup>1</sup>J.W.N. and N.S. contributed equally to this work.</p></fn></author-notes><pub-date pub-type="ppub"><day>28</day><month>4</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>6</day><month>4</month><year>2015</year></pub-date><pub-date pub-type="pmc-release"><day>6</day><month>4</month><year>2015</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>112</volume><issue>17</issue><fpage>5389</fpage><lpage>5394</lpage><permissions><license license-type="open-access"><license-p>Freely available online through the PNAS open access option.</license-p></license></permissions><self-uri xlink:title="pdf" xlink:href="pnas.201419264.pdf"></self-uri><related-article id="d35e199" related-article-type="companion" ext-link-type="doi" xlink:href="10.1073/pnas.1419328112"></related-article><abstract abstract-type="executive-summary"><title>Significance</title><p>The cyclic dinucleotides c-di-GMP and c-di-AMP are responsible for controlling broad changes in cell phenotypes during the life cycles of many bacterial species. To date, riboswitches that sense c-di-GMP and c-di-AMP have been discovered. The genomic locations of riboswitches reveal numerous genes that are controlled by these signaling compounds and thereby reveal the biological processes that are regulated. Herein, we report that a subset of conserved noncoding RNA domains previously annotated as c-di-GMP-I riboswitches in fact bind the newly discovered second messenger c-AMP-GMP. These riboswitches control many genes involved in the utilization of extracellular iron(III) oxide as an electron sink by various <italic>Geobacter</italic> species. Our findings reveal additional roles for this recently discovered signaling molecule.</p></abstract><abstract><p>Major changes in bacterial physiology including biofilm and spore formation involve signaling by the cyclic dinucleotides c-di-GMP and c-di-AMP. Recently, another second messenger dinucleotide, c-AMP-GMP, was found to control chemotaxis and colonization by <italic>Vibrio cholerae</italic>. We have identified a superregulon of genes controlled by c-AMP-GMP in numerous Deltaproteobacteria, including <italic>Geobacter</italic> species that use extracellular insoluble metal oxides as terminal electron acceptors. This exoelectrogenic process has been studied for its possible utility in energy production and bioremediation. Many genes involved in adhesion, pilin formation, and others that are important for exoelectrogenesis are controlled by members of a variant riboswitch class that selectively bind c-AMP-GMP. These RNAs constitute, to our knowledge, the first known specific receptors for c-AMP-GMP and reveal that this molecule is used by many bacteria to control specialized physiological processes.</p></abstract><kwd-group><kwd>riboswitch</kwd><kwd><italic>Geobacter</italic></kwd><kwd>GEMM</kwd><kwd>c-di-GMP</kwd><kwd>second messenger</kwd></kwd-group><funding-group><award-group id="gs1"><funding-source id="sp1">Howard Hughes Medical Institute (HHMI)<named-content content-type="funder-id">100000011</named-content></funding-source><award-id rid="sp1">HHMI</award-id></award-group><award-group id="gs2"><funding-source id="sp2">HHS | National Institutes of Health (NIH)<named-content content-type="funder-id">100000002</named-content></funding-source><award-id rid="sp2">GM022778</award-id></award-group><award-group id="gs3"><funding-source id="sp3">HHS | National Institutes of Health</funding-source><award-id rid="sp3">DE022340</award-id></award-group><award-group id="gs4"><funding-source id="sp4">Deutsche Forschungsgemeinschaft (DFG)<named-content content-type="funder-id">501100001659</named-content></funding-source><award-id rid="sp4">DFG LU1889/1-1</award-id></award-group><award-group id="gs5"><funding-source id="sp5">HHS | National Institutes of Health (NIH)<named-content content-type="funder-id">100000002</named-content></funding-source><award-id rid="sp5">T32-GM007223</award-id></award-group></funding-group><counts><page-count count="6"></page-count></counts></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Breaker, Ronald R" sort="Breaker, Ronald R" uniqKey="Breaker R" first="Ronald R." last="Breaker">Ronald R. Breaker</name><name sortKey="Lunse, Christina E" sort="Lunse, Christina E" uniqKey="Lunse C" first="Christina E." last="Lünse">Christina E. Lünse</name><name sortKey="Mccown, Phillip J" sort="Mccown, Phillip J" uniqKey="Mccown P" first="Phillip J." last="Mccown">Phillip J. Mccown</name><name sortKey="Nelson, James W" sort="Nelson, James W" uniqKey="Nelson J" first="James W." last="Nelson">James W. Nelson</name><name sortKey="Phillips, Grace E" sort="Phillips, Grace E" uniqKey="Phillips G" first="Grace E." last="Phillips">Grace E. Phillips</name><name sortKey="Stav, Shira" sort="Stav, Shira" uniqKey="Stav S" first="Shira" last="Stav">Shira Stav</name><name sortKey="Sudarsan, Narasimhan" sort="Sudarsan, Narasimhan" uniqKey="Sudarsan N" first="Narasimhan" last="Sudarsan">Narasimhan Sudarsan</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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