Cloning and sequence analysis of a cDNA encoding rice glutaredoxin.
Identifieur interne : 001251 ( Main/Exploration ); précédent : 001250; suivant : 001252Cloning and sequence analysis of a cDNA encoding rice glutaredoxin.
Auteurs : K. Minakuchi [Japon] ; T. Yabushita ; T. Masumura ; K. Ichihara ; K. TanakaSource :
- FEBS letters [ 0014-5793 ] ; 1994.
Descripteurs français
- KwdFr :
- ADN complémentaire (analyse), ADN complémentaire (biosynthèse), Animaux (MeSH), Banque de gènes (MeSH), Biosynthèse des protéines (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Gènes de plante (MeSH), Oryza (génétique), Oryza (métabolisme), Oxidoreductases (biosynthèse), Oxidoreductases (génétique), Protein-disulfide reductase (glutathione) (MeSH), Protéines (génétique), Protéines de fusion recombinantes (biosynthèse), Protéines végétales (biosynthèse), Similitude de séquences d'acides aminés (MeSH), Suidae (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- analyse : ADN complémentaire.
- biosynthèse : ADN complémentaire, Oxidoreductases, Protéines de fusion recombinantes, Protéines végétales.
- génétique : Oryza, Oxidoreductases, Protéines.
- métabolisme : Oryza.
- Animaux, Banque de gènes, Biosynthèse des protéines, Clonage moléculaire, Données de séquences moléculaires, Glutarédoxines, Gènes de plante, Protein-disulfide reductase (glutathione), Similitude de séquences d'acides aminés, Suidae, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), DNA, Complementary (analysis), DNA, Complementary (biosynthesis), Gene Library (MeSH), Genes, Plant (MeSH), Glutaredoxins (MeSH), Molecular Sequence Data (MeSH), Oryza (genetics), Oryza (metabolism), Oxidoreductases (biosynthesis), Oxidoreductases (genetics), Plant Proteins (biosynthesis), Protein Biosynthesis (MeSH), Protein Disulfide Reductase (Glutathione) (MeSH), Proteins (genetics), Recombinant Fusion Proteins (biosynthesis), Sequence Homology, Amino Acid (MeSH), Swine (MeSH).
- MESH :
- chemical , analysis : DNA, Complementary.
- chemical , biosynthesis : DNA, Complementary, Oxidoreductases, Plant Proteins, Recombinant Fusion Proteins.
- genetics : Oryza, Oxidoreductases, Proteins.
- metabolism : Oryza.
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Gene Library, Genes, Plant, Glutaredoxins, Molecular Sequence Data, Protein Biosynthesis, Protein Disulfide Reductase (Glutathione), Sequence Homology, Amino Acid, Swine.
Abstract
A full-length cDNA clone (RASC8) encoding glutaredoxin (thioltransferase) was isolated from a cDNA library of an aleurone layer prepared from a developing seed of rice (Oryza sativa L.). RASC8, 568bp in length, contained an ATG codon and two possible polyadenylation signals, and encoded 112 amino acid residues. Cys-Pro-Phe-Cys, which is the active site and a highly conserved sequence among thioltransferases, was found in the deduced amino acid sequence. RASC8 was introduced into an expression vector pMALc2 and the translated product possessed thioltransferase activity.
DOI: 10.1016/0014-5793(94)80264-5
PubMed: 8287970
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Masumura</name></author><author><name sortKey="Ichihara, K" sort="Ichihara, K" uniqKey="Ichihara K" first="K" last="Ichihara">K. Ichihara</name></author><author><name sortKey="Tanaka, K" sort="Tanaka, K" uniqKey="Tanaka K" first="K" last="Tanaka">K. 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Minakuchi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, College of Agriculture, Kyoto Prefectural University, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biochemistry, College of Agriculture, Kyoto Prefectural University</wicri:regionArea><wicri:noRegion>Kyoto Prefectural University</wicri:noRegion></affiliation></author><author><name sortKey="Yabushita, T" sort="Yabushita, T" uniqKey="Yabushita T" first="T" last="Yabushita">T. Yabushita</name></author><author><name sortKey="Masumura, T" sort="Masumura, T" uniqKey="Masumura T" first="T" last="Masumura">T. Masumura</name></author><author><name sortKey="Ichihara, K" sort="Ichihara, K" uniqKey="Ichihara K" first="K" last="Ichihara">K. Ichihara</name></author><author><name sortKey="Tanaka, K" sort="Tanaka, K" uniqKey="Tanaka K" first="K" last="Tanaka">K. Tanaka</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Base Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>DNA, Complementary (analysis)</term><term>DNA, Complementary (biosynthesis)</term><term>Gene Library (MeSH)</term><term>Genes, Plant (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oryza (genetics)</term><term>Oryza (metabolism)</term><term>Oxidoreductases (biosynthesis)</term><term>Oxidoreductases (genetics)</term><term>Plant Proteins (biosynthesis)</term><term>Protein Biosynthesis (MeSH)</term><term>Protein Disulfide Reductase (Glutathione) (MeSH)</term><term>Proteins (genetics)</term><term>Recombinant Fusion Proteins (biosynthesis)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Swine (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (analyse)</term><term>ADN complémentaire (biosynthèse)</term><term>Animaux (MeSH)</term><term>Banque de gènes (MeSH)</term><term>Biosynthèse des protéines (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Gènes de plante (MeSH)</term><term>Oryza (génétique)</term><term>Oryza (métabolisme)</term><term>Oxidoreductases (biosynthèse)</term><term>Oxidoreductases (génétique)</term><term>Protein-disulfide reductase (glutathione) (MeSH)</term><term>Protéines (génétique)</term><term>Protéines de fusion recombinantes (biosynthèse)</term><term>Protéines végétales (biosynthèse)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Suidae (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>DNA, Complementary</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>DNA, Complementary</term><term>Oxidoreductases</term><term>Plant Proteins</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>ADN complémentaire</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>ADN complémentaire</term><term>Oxidoreductases</term><term>Protéines de fusion recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Oryza</term><term>Oxidoreductases</term><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oryza</term><term>Oxidoreductases</term><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Oryza</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oryza</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Gene Library</term><term>Genes, Plant</term><term>Glutaredoxins</term><term>Molecular Sequence Data</term><term>Protein Biosynthesis</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Sequence Homology, Amino Acid</term><term>Swine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Banque de gènes</term><term>Biosynthèse des protéines</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Gènes de plante</term><term>Protein-disulfide reductase (glutathione)</term><term>Similitude de séquences d'acides aminés</term><term>Suidae</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A full-length cDNA clone (RASC8) encoding glutaredoxin (thioltransferase) was isolated from a cDNA library of an aleurone layer prepared from a developing seed of rice (Oryza sativa L.). RASC8, 568bp in length, contained an ATG codon and two possible polyadenylation signals, and encoded 112 amino acid residues. Cys-Pro-Phe-Cys, which is the active site and a highly conserved sequence among thioltransferases, was found in the deduced amino acid sequence. RASC8 was introduced into an expression vector pMALc2 and the translated product possessed thioltransferase activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8287970</PMID><DateCompleted><Year>1994</Year><Month>02</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>337</Volume><Issue>2</Issue><PubDate><Year>1994</Year><Month>Jan</Month><Day>10</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Cloning and sequence analysis of a cDNA encoding rice glutaredoxin.</ArticleTitle><Pagination><MedlinePgn>157-60</MedlinePgn></Pagination><Abstract><AbstractText>A full-length cDNA clone (RASC8) encoding glutaredoxin (thioltransferase) was isolated from a cDNA library of an aleurone layer prepared from a developing seed of rice (Oryza sativa L.). RASC8, 568bp in length, contained an ATG codon and two possible polyadenylation signals, and encoded 112 amino acid residues. Cys-Pro-Phe-Cys, which is the active site and a highly conserved sequence among thioltransferases, was found in the deduced amino acid sequence. RASC8 was introduced into an expression vector pMALc2 and the translated product possessed thioltransferase activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Minakuchi</LastName><ForeName>K</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, College of Agriculture, Kyoto Prefectural University, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yabushita</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Masumura</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Ichihara</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Tanaka</LastName><ForeName>K</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>X77150</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><GeneSymbolList><GeneSymbol>RASC8</GeneSymbol></GeneSymbolList><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, 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MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>1</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1994</Year><Month>1</Month><Day>10</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>1</Month><Day>10</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8287970</ArticleId><ArticleId IdType="pii">0014-5793(94)80264-5</ArticleId><ArticleId 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Ichihara</name><name sortKey="Masumura, T" sort="Masumura, T" uniqKey="Masumura T" first="T" last="Masumura">T. Masumura</name><name sortKey="Tanaka, K" sort="Tanaka, K" uniqKey="Tanaka K" first="K" last="Tanaka">K. Tanaka</name><name sortKey="Yabushita, T" sort="Yabushita, T" uniqKey="Yabushita T" first="T" last="Yabushita">T. Yabushita</name></noCountry><country name="Japon"><noRegion><name sortKey="Minakuchi, K" sort="Minakuchi, K" uniqKey="Minakuchi K" first="K" last="Minakuchi">K. Minakuchi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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