A membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication.
Identifieur interne : 000A64 ( Main/Exploration ); précédent : 000A63; suivant : 000A65A membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication.
Auteurs : Ling Meng [États-Unis] ; Joshua H. Wong ; Lewis J. Feldman ; Peggy G. Lemaux ; Bob B. BuchananSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2010.
Descripteurs français
- KwdFr :
- Arabidopsis (croissance et développement), Arabidopsis (génétique), Communication cellulaire (MeSH), Conformation des protéines (MeSH), Cystéine (génétique), Glycine (génétique), Membrane cellulaire (métabolisme), Mutation (MeSH), Plastes (métabolisme), Protéines d'Arabidopsis (composition chimique), Protéines d'Arabidopsis (génétique), Protéines d'Arabidopsis (physiologie), Séquence d'acides aminés (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (génétique), Thiorédoxines (physiologie).
- MESH :
- composition chimique : Protéines d'Arabidopsis, Thiorédoxines.
- croissance et développement : Arabidopsis.
- génétique : Arabidopsis, Cystéine, Glycine, Protéines d'Arabidopsis, Thiorédoxines.
- métabolisme : Membrane cellulaire, Plastes.
- physiologie : Protéines d'Arabidopsis, Thiorédoxines.
- Communication cellulaire, Conformation des protéines, Mutation, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Arabidopsis (genetics), Arabidopsis (growth & development), Arabidopsis Proteins (chemistry), Arabidopsis Proteins (genetics), Arabidopsis Proteins (physiology), Cell Communication (MeSH), Cell Membrane (metabolism), Cysteine (genetics), Glycine (genetics), Mutation (MeSH), Plastids (metabolism), Protein Conformation (MeSH), Thioredoxins (chemistry), Thioredoxins (genetics), Thioredoxins (physiology).
- MESH :
- chemical , chemistry : Arabidopsis Proteins, Thioredoxins.
- genetics : Arabidopsis, Arabidopsis Proteins, Cysteine, Glycine, Thioredoxins.
- growth & development : Arabidopsis.
- metabolism : Cell Membrane, Plastids.
- chemical , physiology : Arabidopsis Proteins, Thioredoxins.
- Amino Acid Sequence, Cell Communication, Mutation, Protein Conformation.
Abstract
Thioredoxins (Trxs) are small ubiquitous regulatory disulfide proteins. Plants have an unusually complex complement of Trxs composed of six well-defined types (Trxs f, m, x, y, h, and o) that reside in different cell compartments and function in an array of processes. The extraplastidic h type consists of multiple members that in general have resisted isolation of a specific phenotype. In analyzing mutant lines in Arabidopsis thaliana, we identified a phenotype of dwarf plants with short roots and small yellowish leaves for AtTrx h9 (henceforth, Trx h9), a member of the Arabidopsis Trx h family. Trx h9 was found to be associated with the plasma membrane and to move from cell to cell. Controls conducted in conjunction with the localization of Trx h9 uncovered another h-type Trx in mitochondria (Trx h2) and a Trx in plastids earlier described as a cytosolic form in tomato. Analysis of Trx h9 revealed a 17-amino acid N-terminal extension in which the second Gly (Gly(2)) and fourth cysteine (Cys(4)) were highly conserved. Mutagenesis experiments demonstrated that Gly(2) was required for membrane binding, possibly via myristoylation. Both Gly(2) and Cys(4) were needed for movement, the latter seemingly for protein structure and palmitoylation. A three-dimensional model was consistent with these predictions as well as with earlier evidence showing that a poplar ortholog is reduced by a glutaredoxin rather than NADP-thioredoxin reductase. In demonstrating the membrane location and intercellular mobility of Trx h9, the present results extend the known boundaries of Trx and suggest a role in cell-to-cell communication.
DOI: 10.1073/pnas.0913759107
PubMed: 20133584
PubMed Central: PMC2840455
Affiliations:
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Wong</name></author><author><name sortKey="Feldman, Lewis J" sort="Feldman, Lewis J" uniqKey="Feldman L" first="Lewis J" last="Feldman">Lewis J. Feldman</name></author><author><name sortKey="Lemaux, Peggy G" sort="Lemaux, Peggy G" uniqKey="Lemaux P" first="Peggy G" last="Lemaux">Peggy G. Lemaux</name></author><author><name sortKey="Buchanan, Bob B" sort="Buchanan, Bob B" uniqKey="Buchanan B" first="Bob B" last="Buchanan">Bob B. Buchanan</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Arabidopsis (genetics)</term><term>Arabidopsis (growth & development)</term><term>Arabidopsis Proteins (chemistry)</term><term>Arabidopsis Proteins (genetics)</term><term>Arabidopsis Proteins (physiology)</term><term>Cell Communication (MeSH)</term><term>Cell Membrane (metabolism)</term><term>Cysteine (genetics)</term><term>Glycine (genetics)</term><term>Mutation (MeSH)</term><term>Plastids (metabolism)</term><term>Protein Conformation (MeSH)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (croissance et développement)</term><term>Arabidopsis (génétique)</term><term>Communication cellulaire (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cystéine (génétique)</term><term>Glycine (génétique)</term><term>Membrane cellulaire (métabolisme)</term><term>Mutation (MeSH)</term><term>Plastes (métabolisme)</term><term>Protéines d'Arabidopsis (composition chimique)</term><term>Protéines d'Arabidopsis (génétique)</term><term>Protéines d'Arabidopsis (physiologie)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Arabidopsis Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines d'Arabidopsis</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arabidopsis</term><term>Arabidopsis Proteins</term><term>Cysteine</term><term>Glycine</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arabidopsis</term><term>Cystéine</term><term>Glycine</term><term>Protéines d'Arabidopsis</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Plastids</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Membrane cellulaire</term><term>Plastes</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines d'Arabidopsis</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Arabidopsis Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cell Communication</term><term>Mutation</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Communication cellulaire</term><term>Conformation des protéines</term><term>Mutation</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thioredoxins (Trxs) are small ubiquitous regulatory disulfide proteins. Plants have an unusually complex complement of Trxs composed of six well-defined types (Trxs f, m, x, y, h, and o) that reside in different cell compartments and function in an array of processes. The extraplastidic h type consists of multiple members that in general have resisted isolation of a specific phenotype. In analyzing mutant lines in Arabidopsis thaliana, we identified a phenotype of dwarf plants with short roots and small yellowish leaves for AtTrx h9 (henceforth, Trx h9), a member of the Arabidopsis Trx h family. Trx h9 was found to be associated with the plasma membrane and to move from cell to cell. Controls conducted in conjunction with the localization of Trx h9 uncovered another h-type Trx in mitochondria (Trx h2) and a Trx in plastids earlier described as a cytosolic form in tomato. Analysis of Trx h9 revealed a 17-amino acid N-terminal extension in which the second Gly (Gly(2)) and fourth cysteine (Cys(4)) were highly conserved. Mutagenesis experiments demonstrated that Gly(2) was required for membrane binding, possibly via myristoylation. Both Gly(2) and Cys(4) were needed for movement, the latter seemingly for protein structure and palmitoylation. A three-dimensional model was consistent with these predictions as well as with earlier evidence showing that a poplar ortholog is reduced by a glutaredoxin rather than NADP-thioredoxin reductase. In demonstrating the membrane location and intercellular mobility of Trx h9, the present results extend the known boundaries of Trx and suggest a role in cell-to-cell communication.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20133584</PMID><DateCompleted><Year>2010</Year><Month>04</Month><Day>05</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>107</Volume><Issue>8</Issue><PubDate><Year>2010</Year><Month>Feb</Month><Day>23</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>A membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication.</ArticleTitle><Pagination><MedlinePgn>3900-5</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.0913759107</ELocationID><Abstract><AbstractText>Thioredoxins (Trxs) are small ubiquitous regulatory disulfide proteins. Plants have an unusually complex complement of Trxs composed of six well-defined types (Trxs f, m, x, y, h, and o) that reside in different cell compartments and function in an array of processes. The extraplastidic h type consists of multiple members that in general have resisted isolation of a specific phenotype. In analyzing mutant lines in Arabidopsis thaliana, we identified a phenotype of dwarf plants with short roots and small yellowish leaves for AtTrx h9 (henceforth, Trx h9), a member of the Arabidopsis Trx h family. Trx h9 was found to be associated with the plasma membrane and to move from cell to cell. Controls conducted in conjunction with the localization of Trx h9 uncovered another h-type Trx in mitochondria (Trx h2) and a Trx in plastids earlier described as a cytosolic form in tomato. Analysis of Trx h9 revealed a 17-amino acid N-terminal extension in which the second Gly (Gly(2)) and fourth cysteine (Cys(4)) were highly conserved. Mutagenesis experiments demonstrated that Gly(2) was required for membrane binding, possibly via myristoylation. Both Gly(2) and Cys(4) were needed for movement, the latter seemingly for protein structure and palmitoylation. A three-dimensional model was consistent with these predictions as well as with earlier evidence showing that a poplar ortholog is reduced by a glutaredoxin rather than NADP-thioredoxin reductase. In demonstrating the membrane location and intercellular mobility of Trx h9, the present results extend the known boundaries of Trx and suggest a role in cell-to-cell communication.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Meng</LastName><ForeName>Ling</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wong</LastName><ForeName>Joshua H</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Feldman</LastName><ForeName>Lewis J</ForeName><Initials>LJ</Initials></Author><Author ValidYN="Y"><LastName>Lemaux</LastName><ForeName>Peggy G</ForeName><Initials>PG</Initials></Author><Author ValidYN="Y"><LastName>Buchanan</LastName><ForeName>Bob B</ForeName><Initials>BB</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType 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Buchanan</name><name sortKey="Feldman, Lewis J" sort="Feldman, Lewis J" uniqKey="Feldman L" first="Lewis J" last="Feldman">Lewis J. Feldman</name><name sortKey="Lemaux, Peggy G" sort="Lemaux, Peggy G" uniqKey="Lemaux P" first="Peggy G" last="Lemaux">Peggy G. Lemaux</name><name sortKey="Wong, Joshua H" sort="Wong, Joshua H" uniqKey="Wong J" first="Joshua H" last="Wong">Joshua H. Wong</name></noCountry><country name="États-Unis"><region name="Californie"><name sortKey="Meng, Ling" sort="Meng, Ling" uniqKey="Meng L" first="Ling" last="Meng">Ling Meng</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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