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            <title xml:lang="en">Chloroplast ribonucleoprotein CP31A is required for editing and stability of specific chloroplast mRNAs</title>
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              <persName>
                <forename type="first">M.</forename>
                <surname>Tillich</surname>
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              <persName>
                <forename type="first">S.L.</forename>
                <surname>Hardel</surname>
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                <forename type="first">U.</forename>
                <surname>Armbruster</surname>
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              <idno type="halauthorid">403589-0</idno>
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                <forename type="first">E.</forename>
                <surname>Delannoy</surname>
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                <forename type="first">J.M.</forename>
                <surname>Gualberto</surname>
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                <surname>Lehwark</surname>
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                <forename type="first">D.</forename>
                <surname>Leister</surname>
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              <persName>
                <forename type="first">I.D.</forename>
                <surname>Small</surname>
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                <surname>Schmitz-Linneweber</surname>
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                <forename>Francine</forename>
                <surname>Noirtin</surname>
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            <idno type="halRefHtml">&lt;i&gt;Proceedings of the National Academy of Sciences of the United States of America&lt;/i&gt;, 2009, 106 (14), pp.6002-6007. &lt;a target="_blank" href="https://dx.doi.org/10.1073/pnas.0808529106"&gt;&amp;#x27E8;10.1073/pnas.0808529106&amp;#x27E9;&lt;/a&gt;</idno>
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            <idno type="stamp" n="SITE-ALSACE">Archive ouverte du site Alsace</idno>
            <idno type="stamp" n="IBMP">Institut de biologie moléculaire des plantes</idno>
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                <title xml:lang="en">Chloroplast ribonucleoprotein CP31A is required for editing and stability of specific chloroplast mRNAs</title>
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                  <persName>
                    <forename type="first">M.</forename>
                    <surname>Tillich</surname>
                  </persName>
                  <idno type="halauthorid">403586-0</idno>
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                <author role="aut">
                  <persName>
                    <forename type="first">S.L.</forename>
                    <surname>Hardel</surname>
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                  <idno type="halauthorid">403587-0</idno>
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                <author role="aut">
                  <persName>
                    <forename type="first">C.</forename>
                    <surname>Kupsch</surname>
                  </persName>
                  <idno type="halauthorid">403588-0</idno>
                </author>
                <author role="aut">
                  <persName>
                    <forename type="first">U.</forename>
                    <surname>Armbruster</surname>
                  </persName>
                  <idno type="halauthorid">403589-0</idno>
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                <author role="aut">
                  <persName>
                    <forename type="first">E.</forename>
                    <surname>Delannoy</surname>
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                  <email type="md5">444849000b6f73c41429a0ee1c402e13</email>
                  <email type="domain">inrae.fr</email>
                  <idno type="idhal" notation="string">etienne-delannoy</idno>
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                <author role="aut">
                  <persName>
                    <forename type="first">J.M.</forename>
                    <surname>Gualberto</surname>
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                  <idno type="halauthorid">179302-0</idno>
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                <author role="aut">
                  <persName>
                    <forename type="first">P.</forename>
                    <surname>Lehwark</surname>
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                  <idno type="halauthorid">403591-0</idno>
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                <author role="aut">
                  <persName>
                    <forename type="first">D.</forename>
                    <surname>Leister</surname>
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                  <idno type="halauthorid">403592-0</idno>
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                <author role="aut">
                  <persName>
                    <forename type="first">I.D.</forename>
                    <surname>Small</surname>
                  </persName>
                  <idno type="halauthorid">403593-0</idno>
                </author>
                <author role="aut">
                  <persName>
                    <forename type="first">C.</forename>
                    <surname>Schmitz-Linneweber</surname>
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                  <idno type="halauthorid">403594-0</idno>
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                <idno type="halJournalId" status="VALID">7969</idno>
                <idno type="issn">0027-8424</idno>
                <idno type="eissn">1091-6490</idno>
                <title level="j">Proceedings of the National Academy of Sciences of the United States of America</title>
                <imprint>
                  <publisher>National Academy of Sciences</publisher>
                  <biblScope unit="volume">106</biblScope>
                  <biblScope unit="issue">14</biblScope>
                  <biblScope unit="pp">6002-6007</biblScope>
                  <date type="datePub">2009</date>
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              <idno type="doi">10.1073/pnas.0808529106</idno>
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            <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 CP31A exhibit highly specific and diverse defects in chloroplast RNA metabolism. First, analysis of cp31a and cp31a/cp31b 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 cp31a mutants detected a virtually complete loss of the chloroplast ndhF 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 cp31a 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>
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