A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes
Identifieur interne : 000544 ( Pmc/Corpus ); précédent : 000543; suivant : 000545A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes
Auteurs : Inger Carlberg ; Maria Hansson ; Thomas Kieselbach ; Wolfgang P. Schröder ; Bertil Andersson ; Alexander V. VenerSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2003.
Abstract
The characteristics of a phosphoprotein with a relative electrophoretic mobility of 12 kDa have been unknown during two decades of studies on redox-dependent protein phosphorylation in plant photosynthetic membranes. Digestion of this protein from spinach thylakoid membranes with trypsin and subsequent tandem nanospray-quadrupole-time-of-flight mass spectrometry of the peptides revealed a protein sequence that did not correspond to any previously known protein. Sequencing of the corresponding cDNA uncovered a gene for a precursor protein with a transit peptide followed by a strongly basic mature protein with a molecular mass of 8,640 Da. Genes encoding homologous proteins were found on chromosome 3 of
Url:
DOI: 10.1073/pnas.0235452100
PubMed: 12524456
PubMed Central: 141069
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PMC:141069Le document en format XML
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<author><name sortKey="Carlberg, Inger" sort="Carlberg, Inger" uniqKey="Carlberg I" first="Inger" last="Carlberg">Inger Carlberg</name>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden;</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Hansson, Maria" sort="Hansson, Maria" uniqKey="Hansson M" first="Maria" last="Hansson">Maria Hansson</name>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Division of Cell Biology, Linköping University, SE-58185 Linköping, Sweden;</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kieselbach, Thomas" sort="Kieselbach, Thomas" uniqKey="Kieselbach T" first="Thomas" last="Kieselbach">Thomas Kieselbach</name>
<affiliation><nlm:aff wicri:cut="; and" id="N0x9cc7030.0x9eed8d0">Department of Medical Nutrition and Biosciences, Karolinska Institute, Novum, SE-14186 Huddinge, Sweden</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Schroder, Wolfgang P" sort="Schroder, Wolfgang P" uniqKey="Schroder W" first="Wolfgang P." last="Schröder">Wolfgang P. Schröder</name>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Department of Biochemistry, Umeå University, SE-90187 Umeå, Sweden</nlm:aff>
</affiliation>
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<author><name sortKey="Andersson, Bertil" sort="Andersson, Bertil" uniqKey="Andersson B" first="Bertil" last="Andersson">Bertil Andersson</name>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden;</nlm:aff>
</affiliation>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Division of Cell Biology, Linköping University, SE-58185 Linköping, Sweden;</nlm:aff>
</affiliation>
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<author><name sortKey="Vener, Alexander V" sort="Vener, Alexander V" uniqKey="Vener A" first="Alexander V." last="Vener">Alexander V. Vener</name>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Division of Cell Biology, Linköping University, SE-58185 Linköping, Sweden;</nlm:aff>
</affiliation>
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<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC141069</idno>
<idno type="RBID">PMC:141069</idno>
<idno type="doi">10.1073/pnas.0235452100</idno>
<date when="2003">2003</date>
<idno type="wicri:Area/Pmc/Corpus">000544</idno>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes</title>
<author><name sortKey="Carlberg, Inger" sort="Carlberg, Inger" uniqKey="Carlberg I" first="Inger" last="Carlberg">Inger Carlberg</name>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden;</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Hansson, Maria" sort="Hansson, Maria" uniqKey="Hansson M" first="Maria" last="Hansson">Maria Hansson</name>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Division of Cell Biology, Linköping University, SE-58185 Linköping, Sweden;</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kieselbach, Thomas" sort="Kieselbach, Thomas" uniqKey="Kieselbach T" first="Thomas" last="Kieselbach">Thomas Kieselbach</name>
<affiliation><nlm:aff wicri:cut="; and" id="N0x9cc7030.0x9eed8d0">Department of Medical Nutrition and Biosciences, Karolinska Institute, Novum, SE-14186 Huddinge, Sweden</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Schroder, Wolfgang P" sort="Schroder, Wolfgang P" uniqKey="Schroder W" first="Wolfgang P." last="Schröder">Wolfgang P. Schröder</name>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Department of Biochemistry, Umeå University, SE-90187 Umeå, Sweden</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Andersson, Bertil" sort="Andersson, Bertil" uniqKey="Andersson B" first="Bertil" last="Andersson">Bertil Andersson</name>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden;</nlm:aff>
</affiliation>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Division of Cell Biology, Linköping University, SE-58185 Linköping, Sweden;</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Vener, Alexander V" sort="Vener, Alexander V" uniqKey="Vener A" first="Alexander V." last="Vener">Alexander V. Vener</name>
<affiliation><nlm:aff id="N0x9cc7030.0x9eed8d0">Division of Cell Biology, Linköping University, SE-58185 Linköping, Sweden;</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="2003">2003</date>
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<front><div type="abstract" xml:lang="en"><p>The characteristics of a phosphoprotein with a relative electrophoretic mobility of 12 kDa have been unknown during two decades of studies on redox-dependent protein phosphorylation in plant photosynthetic membranes. Digestion of this protein from spinach thylakoid membranes with trypsin and subsequent tandem nanospray-quadrupole-time-of-flight mass spectrometry of the peptides revealed a protein sequence that did not correspond to any previously known protein. Sequencing of the corresponding cDNA uncovered a gene for a precursor protein with a transit peptide followed by a strongly basic mature protein with a molecular mass of 8,640 Da. Genes encoding homologous proteins were found on chromosome 3 of <italic>Arabidopsis</italic>
and rice as well as in ESTs from 20 different plant species, but not from any other organisms. The protein can be released from the membrane with high salt and is also partially released in response to light-induced phosphorylation of thylakoids, in contrast to all other known thylakoid phosphoproteins, which are integral to the membrane. On the basis of its properties, this plant-specific protein is named thylakoid soluble phosphoprotein of 9 kDa (TSP9). Mass spectrometric analyses revealed the existence of non-, mono-, di-, and triphosphorylated forms of TSP9 and phosphorylation of three distinct threonine residues in the central part of the protein. The phosphorylation and release of TSP9 from the photosynthetic membrane on illumination favor participation of this basic protein in cell signaling and regulation of plant gene expression in response to changing light conditions.</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="publisher-id">PNAS</journal-id>
<journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title>
<issn pub-type="ppub">0027-8424</issn>
<issn pub-type="epub">1091-6490</issn>
<publisher><publisher-name>The National Academy of Sciences</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">12524456</article-id>
<article-id pub-id-type="pmc">141069</article-id>
<article-id pub-id-type="publisher-id">0235452100</article-id>
<article-id pub-id-type="publisher-id">5452</article-id>
<article-id pub-id-type="doi">10.1073/pnas.0235452100</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>A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Carlberg</surname>
<given-names>Inger</given-names>
</name>
<xref ref-type="aff" rid="N0x9cc7030.0x9eed8d0">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Hansson</surname>
<given-names>Maria</given-names>
</name>
<xref ref-type="aff" rid="N0x9cc7030.0x9eed8d0">†</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kieselbach</surname>
<given-names>Thomas</given-names>
</name>
<xref ref-type="aff" rid="N0x9cc7030.0x9eed8d0">‡</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Schröder</surname>
<given-names>Wolfgang P.</given-names>
</name>
<xref ref-type="aff" rid="N0x9cc7030.0x9eed8d0">§</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Andersson</surname>
<given-names>Bertil</given-names>
</name>
<xref ref-type="aff" rid="N0x9cc7030.0x9eed8d0">*</xref>
<xref ref-type="aff" rid="N0x9cc7030.0x9eed8d0">†</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Vener</surname>
<given-names>Alexander V.</given-names>
</name>
<xref ref-type="aff" rid="N0x9cc7030.0x9eed8d0">†</xref>
<xref ref-type="author-notes" rid="FN154">¶</xref>
</contrib>
</contrib-group>
<aff id="N0x9cc7030.0x9eed8d0"><label>†</label>
Division of Cell Biology, Linköping University, SE-58185 Linköping, Sweden;<label>*</label>
Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden;<label>‡</label>
Department of Medical Nutrition and Biosciences, Karolinska Institute, Novum, SE-14186 Huddinge, Sweden; and<label>§</label>
Department of Biochemistry, Umeå University, SE-90187 Umeå, Sweden</aff>
<author-notes><fn id="FN154"><label>¶</label>
<p>To whom correspondence should be addressed. E-mail: <email>aleve@ibk.liu.se</email>
.</p>
</fn>
<fn><p>Edited by George H. Lorimer, University of Maryland, College Park, MD, and approved November 22, 2002</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><day>21</day>
<month>1</month>
<year>2003</year>
</pub-date>
<pub-date pub-type="epub"><day>10</day>
<month>1</month>
<year>2003</year>
</pub-date>
<volume>100</volume>
<issue>2</issue>
<fpage>757</fpage>
<lpage>762</lpage>
<history><date date-type="received"><day>8</day>
<month>9</month>
<year>2002</year>
</date>
</history>
<copyright-statement>Copyright © 2003, The National Academy of Sciences</copyright-statement>
<copyright-year>2003</copyright-year>
<abstract><p>The characteristics of a phosphoprotein with a relative electrophoretic mobility of 12 kDa have been unknown during two decades of studies on redox-dependent protein phosphorylation in plant photosynthetic membranes. Digestion of this protein from spinach thylakoid membranes with trypsin and subsequent tandem nanospray-quadrupole-time-of-flight mass spectrometry of the peptides revealed a protein sequence that did not correspond to any previously known protein. Sequencing of the corresponding cDNA uncovered a gene for a precursor protein with a transit peptide followed by a strongly basic mature protein with a molecular mass of 8,640 Da. Genes encoding homologous proteins were found on chromosome 3 of <italic>Arabidopsis</italic>
and rice as well as in ESTs from 20 different plant species, but not from any other organisms. The protein can be released from the membrane with high salt and is also partially released in response to light-induced phosphorylation of thylakoids, in contrast to all other known thylakoid phosphoproteins, which are integral to the membrane. On the basis of its properties, this plant-specific protein is named thylakoid soluble phosphoprotein of 9 kDa (TSP9). Mass spectrometric analyses revealed the existence of non-, mono-, di-, and triphosphorylated forms of TSP9 and phosphorylation of three distinct threonine residues in the central part of the protein. The phosphorylation and release of TSP9 from the photosynthetic membrane on illumination favor participation of this basic protein in cell signaling and regulation of plant gene expression in response to changing light conditions.</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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