Plant methionine sulfoxide reductase A and B multigenic families.
Identifieur interne : 003D49 ( Main/Exploration ); précédent : 003D48; suivant : 003D50Plant methionine sulfoxide reductase A and B multigenic families.
Auteurs : Nicolas Rouhier [France] ; Christina Vieira Dos Santos ; Lionel Tarrago ; Pascal ReySource :
- Photosynthesis research [ 0166-8595 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Plantes.
- génétique : Oxidoreductases, Plantes.
- métabolisme : Oxidoreductases.
- Famille multigénique, Methionine Sulfoxide Reductases.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Oxidoreductases.
- chemical , metabolism : Oxidoreductases.
- chemical : Methionine Sulfoxide Reductases.
- enzymology : Plants.
- genetics : Plants.
- Multigene Family.
Abstract
Methionine oxidation to methionine sulfoxide (MetSo), which results in modification of activity and conformation for many proteins, is reversed by an enzyme present in most organisms and termed as methionine sulfoxide reductase (MSR). On the basis of substrate stereospecificity, two types of MSR, A and B, that do not share any sequence similarity, have been identified. In the present review, we first compare the multigenic MSR families in the three plant species for which the genome is fully sequenced: Arabidopsis thaliana, Oryza sativa, and Populus trichocarpa. The MSR gene content is larger in A. thaliana (five MSRAs and nine MSRBs) compared to P. trichocarpa (five MSRAs and four MSRBs) and O. sativa (four MSRAs and three MSRBs). A complete classification based on gene structure, sequence identity, position of conserved reactive cysteines and predicted subcellular localization is proposed. On the basis of in silico and experimental data originating mainly from Arabidopsis, we report that some MSR genes display organ-specific expression patterns and that those encoding plastidic MSRs are highly expressed in photosynthetic organs. We also show that the expression of numerous MSR genes is enhanced by environmental conditions known to generate oxidative stress. Thioredoxins (TRXs) constitute very likely physiological electron donors to plant MSR proteins for the catalysis of MetSO reduction, but the specificity between the numerous TRXs and methionine sulfoxide reductases (MSRs) present in plants remains to be investigated. The essential role of plant MSRs in protection against oxidative damage has been recently demonstrated on transgenic Arabidopsis plants modified in the content of cytosolic or plastidic MSRA.
DOI: 10.1007/s11120-006-9097-1
PubMed: 17031545
Affiliations:
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scheme="MESH" qualifier="genetics" xml:lang="en"><term>Plants</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oxidoreductases</term><term>Plantes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Multigene Family</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Famille multigénique</term><term>Methionine Sulfoxide Reductases</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Methionine oxidation to methionine sulfoxide (MetSo), which results in modification of activity and conformation for many proteins, is reversed by an enzyme present in most organisms and termed as methionine sulfoxide reductase (MSR). On the basis of substrate stereospecificity, two types of MSR, A and B, that do not share any sequence similarity, have been identified. In the present review, we first compare the multigenic MSR families in the three plant species for which the genome is fully sequenced: Arabidopsis thaliana, Oryza sativa, and Populus trichocarpa. The MSR gene content is larger in A. thaliana (five MSRAs and nine MSRBs) compared to P. trichocarpa (five MSRAs and four MSRBs) and O. sativa (four MSRAs and three MSRBs). A complete classification based on gene structure, sequence identity, position of conserved reactive cysteines and predicted subcellular localization is proposed. On the basis of in silico and experimental data originating mainly from Arabidopsis, we report that some MSR genes display organ-specific expression patterns and that those encoding plastidic MSRs are highly expressed in photosynthetic organs. We also show that the expression of numerous MSR genes is enhanced by environmental conditions known to generate oxidative stress. Thioredoxins (TRXs) constitute very likely physiological electron donors to plant MSR proteins for the catalysis of MetSO reduction, but the specificity between the numerous TRXs and methionine sulfoxide reductases (MSRs) present in plants remains to be investigated. The essential role of plant MSRs in protection against oxidative damage has been recently demonstrated on transgenic Arabidopsis plants modified in the content of cytosolic or plastidic MSRA.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17031545</PMID><DateCompleted><Year>2007</Year><Month>03</Month><Day>28</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0166-8595</ISSN><JournalIssue CitedMedium="Print"><Volume>89</Volume><Issue>2-3</Issue><PubDate><Year>2006</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Photosynthesis research</Title><ISOAbbreviation>Photosynth Res</ISOAbbreviation></Journal><ArticleTitle>Plant methionine sulfoxide reductase A and B multigenic families.</ArticleTitle><Pagination><MedlinePgn>247-62</MedlinePgn></Pagination><Abstract><AbstractText>Methionine oxidation to methionine sulfoxide (MetSo), which results in modification of activity and conformation for many proteins, is reversed by an enzyme present in most organisms and termed as methionine sulfoxide reductase (MSR). On the basis of substrate stereospecificity, two types of MSR, A and B, that do not share any sequence similarity, have been identified. In the present review, we first compare the multigenic MSR families in the three plant species for which the genome is fully sequenced: Arabidopsis thaliana, Oryza sativa, and Populus trichocarpa. The MSR gene content is larger in A. thaliana (five MSRAs and nine MSRBs) compared to P. trichocarpa (five MSRAs and four MSRBs) and O. sativa (four MSRAs and three MSRBs). A complete classification based on gene structure, sequence identity, position of conserved reactive cysteines and predicted subcellular localization is proposed. On the basis of in silico and experimental data originating mainly from Arabidopsis, we report that some MSR genes display organ-specific expression patterns and that those encoding plastidic MSRs are highly expressed in photosynthetic organs. We also show that the expression of numerous MSR genes is enhanced by environmental conditions known to generate oxidative stress. Thioredoxins (TRXs) constitute very likely physiological electron donors to plant MSR proteins for the catalysis of MetSO reduction, but the specificity between the numerous TRXs and methionine sulfoxide reductases (MSRs) present in plants remains to be investigated. The essential role of plant MSRs in protection against oxidative damage has been recently demonstrated on transgenic Arabidopsis plants modified in the content of cytosolic or plastidic MSRA.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>IFR 110, Génomique Ecologie et Ecophysiologie Fonctionnelles, Unité Mixte de Recherches 1136 Interaction arbres microorganismes INRA Université Henri Poincaré, BP 239, Vandoeuvre-lès-Nancy Cedex, 54506, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vieira Dos Santos</LastName><ForeName>Christina</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Tarrago</LastName><ForeName>Lionel</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Rey</LastName><ForeName>Pascal</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>09</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Photosynth Res</MedlineTA><NlmUniqueID>100954728</NlmUniqueID><ISSNLinking>0166-8595</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.-</RegistryNumber><NameOfSubstance UI="D051150">Methionine Sulfoxide Reductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.11</RegistryNumber><NameOfSubstance UI="C027219">methionine sulfoxide 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Poincaré</li></orgName></list><tree><noCountry><name sortKey="Rey, Pascal" sort="Rey, Pascal" uniqKey="Rey P" first="Pascal" last="Rey">Pascal Rey</name><name sortKey="Tarrago, Lionel" sort="Tarrago, Lionel" uniqKey="Tarrago L" first="Lionel" last="Tarrago">Lionel Tarrago</name><name sortKey="Vieira Dos Santos, Christina" sort="Vieira Dos Santos, Christina" uniqKey="Vieira Dos Santos C" first="Christina" last="Vieira Dos Santos">Christina Vieira Dos Santos</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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