Links to Exploration step
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Chloroplast ribonucleoprotein CP31A is required for editing and stability of specific chloroplast mRNAs</title><author><name sortKey="Tillich, Michael" sort="Tillich, Michael" uniqKey="Tillich M" first="Michael" last="Tillich">Michael Tillich</name><affiliation><nlm:aff id="aff1">Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</nlm:aff></affiliation></author><author><name sortKey="Hardel, Simone L" sort="Hardel, Simone L" uniqKey="Hardel S" first="Simone L." last="Hardel">Simone L. Hardel</name><affiliation><nlm:aff id="aff1">Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</nlm:aff></affiliation></author><author><name sortKey="Kupsch, Christiane" sort="Kupsch, Christiane" uniqKey="Kupsch C" first="Christiane" last="Kupsch">Christiane Kupsch</name><affiliation><nlm:aff id="aff1">Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</nlm:aff></affiliation></author><author><name sortKey="Armbruster, Ute" sort="Armbruster, Ute" uniqKey="Armbruster U" first="Ute" last="Armbruster">Ute Armbruster</name><affiliation><nlm:aff id="aff2">Lehrstuhl für Botanik, Department Biologie I;</nlm:aff></affiliation></author><author><name sortKey="Delannoy, Etienne" sort="Delannoy, Etienne" uniqKey="Delannoy E" first="Etienne" last="Delannoy">Etienne Delannoy</name><affiliation><nlm:aff wicri:cut="; and" id="aff4">Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Perth, Australia</nlm:aff></affiliation></author><author><name sortKey="Gualberto, Jose M" sort="Gualberto, Jose M" uniqKey="Gualberto J" first="José M." last="Gualberto">José M. Gualberto</name><affiliation><nlm:aff id="aff5">Institut de Biologie Moléculaire des Plantes du Centre National de la Recherche Scientifique, Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg Cedex, France</nlm:aff></affiliation></author><author><name sortKey="Lehwark, Pascal" sort="Lehwark, Pascal" uniqKey="Lehwark P" first="Pascal" last="Lehwark">Pascal Lehwark</name><affiliation><nlm:aff id="aff1">Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</nlm:aff></affiliation></author><author><name sortKey="Leister, Dario" sort="Leister, Dario" uniqKey="Leister D" first="Dario" last="Leister">Dario Leister</name><affiliation><nlm:aff id="aff2">Lehrstuhl für Botanik, Department Biologie I;</nlm:aff></affiliation></author><author><name sortKey="Small, Ian D" sort="Small, Ian D" uniqKey="Small I" first="Ian D." last="Small">Ian D. Small</name><affiliation><nlm:aff wicri:cut="; and" id="aff4">Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Perth, Australia</nlm:aff></affiliation></author><author><name sortKey="Schmitz Linneweber, Christian" sort="Schmitz Linneweber, Christian" uniqKey="Schmitz Linneweber C" first="Christian" last="Schmitz-Linneweber">Christian Schmitz-Linneweber</name><affiliation><nlm:aff id="aff1">Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">19297624</idno><idno type="pmc">2667074</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2667074</idno><idno type="RBID">PMC:2667074</idno><idno type="doi">10.1073/pnas.0808529106</idno><date when="2009">2009</date><idno type="wicri:Area/Pmc/Corpus">001B25</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001B25</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Chloroplast ribonucleoprotein CP31A is required for editing and stability of specific chloroplast mRNAs</title><author><name sortKey="Tillich, Michael" sort="Tillich, Michael" uniqKey="Tillich M" first="Michael" last="Tillich">Michael Tillich</name><affiliation><nlm:aff id="aff1">Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</nlm:aff></affiliation></author><author><name sortKey="Hardel, Simone L" sort="Hardel, Simone L" uniqKey="Hardel S" first="Simone L." last="Hardel">Simone L. Hardel</name><affiliation><nlm:aff id="aff1">Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</nlm:aff></affiliation></author><author><name sortKey="Kupsch, Christiane" sort="Kupsch, Christiane" uniqKey="Kupsch C" first="Christiane" last="Kupsch">Christiane Kupsch</name><affiliation><nlm:aff id="aff1">Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</nlm:aff></affiliation></author><author><name sortKey="Armbruster, Ute" sort="Armbruster, Ute" uniqKey="Armbruster U" first="Ute" last="Armbruster">Ute Armbruster</name><affiliation><nlm:aff id="aff2">Lehrstuhl für Botanik, Department Biologie I;</nlm:aff></affiliation></author><author><name sortKey="Delannoy, Etienne" sort="Delannoy, Etienne" uniqKey="Delannoy E" first="Etienne" last="Delannoy">Etienne Delannoy</name><affiliation><nlm:aff wicri:cut="; and" id="aff4">Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Perth, Australia</nlm:aff></affiliation></author><author><name sortKey="Gualberto, Jose M" sort="Gualberto, Jose M" uniqKey="Gualberto J" first="José M." last="Gualberto">José M. Gualberto</name><affiliation><nlm:aff id="aff5">Institut de Biologie Moléculaire des Plantes du Centre National de la Recherche Scientifique, Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg Cedex, France</nlm:aff></affiliation></author><author><name sortKey="Lehwark, Pascal" sort="Lehwark, Pascal" uniqKey="Lehwark P" first="Pascal" last="Lehwark">Pascal Lehwark</name><affiliation><nlm:aff id="aff1">Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</nlm:aff></affiliation></author><author><name sortKey="Leister, Dario" sort="Leister, Dario" uniqKey="Leister D" first="Dario" last="Leister">Dario Leister</name><affiliation><nlm:aff id="aff2">Lehrstuhl für Botanik, Department Biologie I;</nlm:aff></affiliation></author><author><name sortKey="Small, Ian D" sort="Small, Ian D" uniqKey="Small I" first="Ian D." last="Small">Ian D. Small</name><affiliation><nlm:aff wicri:cut="; and" id="aff4">Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Perth, Australia</nlm:aff></affiliation></author><author><name sortKey="Schmitz Linneweber, Christian" sort="Schmitz Linneweber, Christian" uniqKey="Schmitz Linneweber C" first="Christian" last="Schmitz-Linneweber">Christian Schmitz-Linneweber</name><affiliation><nlm:aff id="aff1">Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</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="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Chloroplast ribonucleoproteins (cpRNPs) are nuclear-encoded, highly abundant, and light-regulated RNA binding proteins. They have been shown to be involved in chloroplast RNA processing and stabilization in vitro and are phylogenetically related to the well-described heterogeneous nuclear ribonucleoproteins (hnRNPs). cpRNPs have been found associated with mRNAs present in chloroplasts and have been regarded as nonspecific stabilizers of chloroplast transcripts. Here, we demonstrate that null mutants of the cpRNP family member <italic>CP31A</italic> exhibit highly specific and diverse defects in chloroplast RNA metabolism. First, analysis of <italic>cp31a</italic> and <italic>cp31a</italic>/<italic>cp31b</italic> double mutants uncovers that these 2 paralogous genes participate nonredundantly in a combinatorial fashion in processing a subset of chloroplast editing sites in vivo. Second, a genome-wide analysis of chloroplast transcript accumulation in <italic>cp31a</italic> mutants detected a virtually complete loss of the chloroplast <italic>ndhF</italic> mRNA and lesser reductions for specific other mRNAs. Fluorescence analyses show that the activity of the NADH dehydrogenase complex, which also includes the NdhF subunit, is defective in <italic>cp31a</italic> mutants. This indicates that cpRNPs are important in vivo for calibrating the expression levels of specific chloroplast mRNAs and impact chloroplast physiology. Taken together, the specificity and combinatorial aspects of cpRNP functions uncovered suggest that these chloroplast proteins are functional equivalents of nucleocytosolic hnRNPs.</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="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">19297624</article-id><article-id pub-id-type="pmc">2667074</article-id><article-id pub-id-type="publisher-id">7076</article-id><article-id pub-id-type="doi">10.1073/pnas.0808529106</article-id><article-categories><subj-group subj-group-type="heading"><subject>Biological Sciences</subject><subj-group><subject>Plant Biology</subject></subj-group></subj-group></article-categories><title-group><article-title>Chloroplast ribonucleoprotein CP31A is required for editing and stability of specific chloroplast mRNAs</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Tillich</surname><given-names>Michael</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>Hardel</surname><given-names>Simone L.</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>Kupsch</surname><given-names>Christiane</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Armbruster</surname><given-names>Ute</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Delannoy</surname><given-names>Etienne</given-names></name><xref ref-type="aff" rid="aff4"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Gualberto</surname><given-names>José M.</given-names></name><xref ref-type="aff" rid="aff5"><sup>d</sup></xref></contrib><contrib contrib-type="author"><name><surname>Lehwark</surname><given-names>Pascal</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Leister</surname><given-names>Dario</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Small</surname><given-names>Ian D.</given-names></name><xref ref-type="aff" rid="aff4"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Schmitz-Linneweber</surname><given-names>Christian</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="corresp" rid="cor1"><sup>2</sup></xref></contrib><aff id="aff1"><sup>a</sup>Institute of Biology, Humboldt-University of Berlin, 10115 Berlin, Germany;</aff><aff id="aff2"><sup>b</sup>Lehrstuhl für Botanik, Department Biologie I;</aff><aff id="aff3">Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany;</aff><aff id="aff4"><sup>c</sup>Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Perth, Australia; and</aff><aff id="aff5"><sup>d</sup>Institut de Biologie Moléculaire des Plantes du Centre National de la Recherche Scientifique, Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg Cedex, France</aff></contrib-group><author-notes><corresp id="cor1"><sup>2</sup>To whom correspondence should be addressed. E-mail: <email>christian.schmitz-linneweber@rz.hu-berlin.de</email></corresp><fn fn-type="edited-by"><p>Edited by Gadi Schuster, Technion-Israel Institute of Technology, Haifa, Israel, and accepted by the Editorial Board January 16, 2009</p></fn><fn fn-type="con"><p>Author contributions: M.T. and C.S.-L. designed research; M.T., S.L.H., C.K., U.A., E.D., J.M.G., and P.L. performed research; M.T., S.L.H., C.K., U.A., E.D., J.M.G., P.L., D.L., I.D.S., and C.S.-L. analyzed data; and C.S.-L. wrote the paper.</p></fn><fn id="FN1" fn-type="equal"><p><sup>1</sup>M.T. and S.L.H. contributed equally to this work.</p></fn></author-notes><pub-date pub-type="ppub"><day>7</day><month>4</month><year>2009</year></pub-date><pub-date pub-type="epub"><day>18</day><month>3</month><year>2009</year></pub-date><volume>106</volume><issue>14</issue><fpage>6002</fpage><lpage>6007</lpage><history><date date-type="received"><day>29</day><month>8</month><year>2008</year></date></history><permissions></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zpq01409006002.pdf"></self-uri><abstract><p>Chloroplast ribonucleoproteins (cpRNPs) are nuclear-encoded, highly abundant, and light-regulated RNA binding proteins. They have been shown to be involved in chloroplast RNA processing and stabilization in vitro and are phylogenetically related to the well-described heterogeneous nuclear ribonucleoproteins (hnRNPs). cpRNPs have been found associated with mRNAs present in chloroplasts and have been regarded as nonspecific stabilizers of chloroplast transcripts. Here, we demonstrate that null mutants of the cpRNP family member <italic>CP31A</italic> exhibit highly specific and diverse defects in chloroplast RNA metabolism. First, analysis of <italic>cp31a</italic> and <italic>cp31a</italic>/<italic>cp31b</italic> double mutants uncovers that these 2 paralogous genes participate nonredundantly in a combinatorial fashion in processing a subset of chloroplast editing sites in vivo. Second, a genome-wide analysis of chloroplast transcript accumulation in <italic>cp31a</italic> mutants detected a virtually complete loss of the chloroplast <italic>ndhF</italic> mRNA and lesser reductions for specific other mRNAs. Fluorescence analyses show that the activity of the NADH dehydrogenase complex, which also includes the NdhF subunit, is defective in <italic>cp31a</italic> mutants. This indicates that cpRNPs are important in vivo for calibrating the expression levels of specific chloroplast mRNAs and impact chloroplast physiology. Taken together, the specificity and combinatorial aspects of cpRNP functions uncovered suggest that these chloroplast proteins are functional equivalents of nucleocytosolic hnRNPs.</p></abstract><kwd-group><kwd><italic>Arabidopsis</italic></kwd><kwd>RNA binding</kwd><kwd>RNA editing</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Asie/explor/AustralieFrV1/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001B25 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 001B25 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Asie
|area= AustralieFrV1
|flux= Pmc
|étape= Corpus
|type= RBID
|clé=
|texte=
}}
| This area was generated with Dilib version V0.6.33. |  |