Cloning and sequencing the cDNA encoding pig liver thioltransferase.
Identifieur interne : 001329 ( Main/Exploration ); précédent : 001328; suivant : 001330Cloning and sequencing the cDNA encoding pig liver thioltransferase.
Auteurs : Y F Yang [États-Unis] ; Z R Gan ; W W WellsSource :
- Gene [ 0378-1119 ] ; 1989.
Descripteurs français
- KwdFr :
- ADN (génétique), Animaux (MeSH), Banque de gènes (MeSH), Clonage moléculaire (MeSH), Codon (génétique), Données de séquences moléculaires (MeSH), Foie (enzymologie), Glutarédoxines (MeSH), Gènes (MeSH), Hybridation d'acides nucléiques (MeSH), Oxidoreductases (génétique), Protein-disulfide reductase (glutathione) (MeSH), Sondes oligonucléotidiques (MeSH), Suidae (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- enzymologie : Foie.
- génétique : ADN, Codon, Oxidoreductases.
- Animaux, Banque de gènes, Clonage moléculaire, Données de séquences moléculaires, Glutarédoxines, Gènes, Hybridation d'acides nucléiques, Protein-disulfide reductase (glutathione), Sondes oligonucléotidiques, Suidae, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), Codon (genetics), DNA (genetics), Gene Library (MeSH), Genes (MeSH), Glutaredoxins (MeSH), Liver (enzymology), Molecular Sequence Data (MeSH), Nucleic Acid Hybridization (MeSH), Oligonucleotide Probes (MeSH), Oxidoreductases (genetics), Protein Disulfide Reductase (Glutathione) (MeSH), Swine (MeSH).
- MESH :
- chemical , genetics : Codon, DNA, Oxidoreductases.
- enzymology : Liver.
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Gene Library, Genes, Glutaredoxins, Molecular Sequence Data, Nucleic Acid Hybridization, Oligonucleotide Probes, Protein Disulfide Reductase (Glutathione), Swine.
Abstract
We report here, the first successful cloning and sequencing of a full-length cDNA gene (TT) encoding the pig liver thioltransferase (TT). The TT cDNA was obtained by screening a commercial (Clonetech) pig liver cDNA library in lambda gt11, using polyclonal antibodies raised in rabbits against pig liver TT. Two positive clones were identified in 3.5 x 10(5) recombinants. For verification, we successfully hybridized three oligodeoxyribonucleotide nucleotide probes, synthesized according to three different regions of the pig liver TT amino acid (aa) sequence, to both of the positive clones. In addition, the size of the TT beta-galactosidase fusion protein, produced by the positive clone, was consistent with the length of the cDNA. The TT cDNA was subcloned into the EcoRI site of M13mp18 replicative form and sequenced by the dideoxy chain-termination method using 35S-labeled nucleotides. The aa sequence deduced from the cDNA sequence is in exact agreement with the previously reported primary aa sequence, except that the N terminus should be N-acetylalanine followed by glutamine, rather than the reverse, as originally interpreted by conventional mass spectrometry fast atom bombardment analysis of the tryptic peptide corresponding to the first 8 aa residues.
DOI: 10.1016/0378-1119(89)90120-0
PubMed: 2583530
Affiliations:
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Le document en format XML
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type="pmid">2583530</idno><idno type="doi">10.1016/0378-1119(89)90120-0</idno><idno type="wicri:Area/Main/Corpus">001322</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001322</idno><idno type="wicri:Area/Main/Curation">001322</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001322</idno><idno type="wicri:Area/Main/Exploration">001322</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Cloning and sequencing the cDNA encoding pig liver thioltransferase.</title><author><name sortKey="Yang, Y F" sort="Yang, Y F" uniqKey="Yang Y" first="Y F" last="Yang">Y F Yang</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824.</nlm:affiliation><orgName type="university">Université d'État du Michigan</orgName><country>États-Unis</country><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Gan, Z R" sort="Gan, Z R" uniqKey="Gan Z" first="Z R" last="Gan">Z R Gan</name></author><author><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></author></analytic><series><title level="j">Gene</title><idno type="ISSN">0378-1119</idno><imprint><date when="1989" type="published">1989</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>Codon (genetics)</term><term>DNA (genetics)</term><term>Gene Library (MeSH)</term><term>Genes (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Liver (enzymology)</term><term>Molecular Sequence Data (MeSH)</term><term>Nucleic Acid Hybridization (MeSH)</term><term>Oligonucleotide Probes (MeSH)</term><term>Oxidoreductases (genetics)</term><term>Protein Disulfide Reductase (Glutathione) (MeSH)</term><term>Swine (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN (génétique)</term><term>Animaux (MeSH)</term><term>Banque de gènes (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Codon (génétique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Foie (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Gènes (MeSH)</term><term>Hybridation d'acides nucléiques (MeSH)</term><term>Oxidoreductases (génétique)</term><term>Protein-disulfide reductase (glutathione) (MeSH)</term><term>Sondes oligonucléotidiques (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="genetics" xml:lang="en"><term>Codon</term><term>DNA</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Foie</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Liver</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN</term><term>Codon</term><term>Oxidoreductases</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</term><term>Glutaredoxins</term><term>Molecular Sequence Data</term><term>Nucleic Acid Hybridization</term><term>Oligonucleotide Probes</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Swine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Banque de gènes</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Gènes</term><term>Hybridation d'acides nucléiques</term><term>Protein-disulfide reductase (glutathione)</term><term>Sondes oligonucléotidiques</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">We report here, the first successful cloning and sequencing of a full-length cDNA gene (TT) encoding the pig liver thioltransferase (TT). The TT cDNA was obtained by screening a commercial (Clonetech) pig liver cDNA library in lambda gt11, using polyclonal antibodies raised in rabbits against pig liver TT. Two positive clones were identified in 3.5 x 10(5) recombinants. For verification, we successfully hybridized three oligodeoxyribonucleotide nucleotide probes, synthesized according to three different regions of the pig liver TT amino acid (aa) sequence, to both of the positive clones. In addition, the size of the TT beta-galactosidase fusion protein, produced by the positive clone, was consistent with the length of the cDNA. The TT cDNA was subcloned into the EcoRI site of M13mp18 replicative form and sequenced by the dideoxy chain-termination method using 35S-labeled nucleotides. The aa sequence deduced from the cDNA sequence is in exact agreement with the previously reported primary aa sequence, except that the N terminus should be N-acetylalanine followed by glutamine, rather than the reverse, as originally interpreted by conventional mass spectrometry fast atom bombardment analysis of the tryptic peptide corresponding to the first 8 aa residues.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2583530</PMID><DateCompleted><Year>1990</Year><Month>01</Month><Day>11</Day></DateCompleted><DateRevised><Year>2019</Year><Month>07</Month><Day>07</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0378-1119</ISSN><JournalIssue CitedMedium="Print"><Volume>83</Volume><Issue>2</Issue><PubDate><Year>1989</Year><Month>Nov</Month><Day>30</Day></PubDate></JournalIssue><Title>Gene</Title><ISOAbbreviation>Gene</ISOAbbreviation></Journal><ArticleTitle>Cloning and sequencing the cDNA encoding pig liver thioltransferase.</ArticleTitle><Pagination><MedlinePgn>339-46</MedlinePgn></Pagination><Abstract><AbstractText>We report here, the first successful cloning and sequencing of a full-length cDNA gene (TT) encoding the pig liver thioltransferase (TT). The TT cDNA was obtained by screening a commercial (Clonetech) pig liver cDNA library in lambda gt11, using polyclonal antibodies raised in rabbits against pig liver TT. Two positive clones were identified in 3.5 x 10(5) recombinants. For verification, we successfully hybridized three oligodeoxyribonucleotide nucleotide probes, synthesized according to three different regions of the pig liver TT amino acid (aa) sequence, to both of the positive clones. In addition, the size of the TT beta-galactosidase fusion protein, produced by the positive clone, was consistent with the length of the cDNA. The TT cDNA was subcloned into the EcoRI site of M13mp18 replicative form and sequenced by the dideoxy chain-termination method using 35S-labeled nucleotides. The aa sequence deduced from the cDNA sequence is in exact agreement with the previously reported primary aa sequence, except that the N terminus should be N-acetylalanine followed by glutamine, rather than the reverse, as originally interpreted by conventional mass spectrometry fast atom bombardment analysis of the tryptic peptide corresponding to the first 8 aa residues.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Y F</ForeName><Initials>YF</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gan</LastName><ForeName>Z R</ForeName><Initials>ZR</Initials></Author><Author ValidYN="Y"><LastName>Wells</LastName><ForeName>W W</ForeName><Initials>WW</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM-38634</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Gene</MedlineTA><NlmUniqueID>7706761</NlmUniqueID><ISSNLinking>0378-1119</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003062">Codon</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015345">Oligonucleotide Probes</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-49-2</RegistryNumber><NameOfSubstance UI="D004247">DNA</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015723" MajorTopicYN="N">Gene Library</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005796" MajorTopicYN="Y">Genes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009693" MajorTopicYN="N">Nucleic Acid Hybridization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015345" MajorTopicYN="N">Oligonucleotide Probes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1989</Year><Month>11</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1989</Year><Month>11</Month><Day>30</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1989</Year><Month>11</Month><Day>30</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2583530</ArticleId><ArticleId IdType="pii">0378-1119(89)90120-0</ArticleId><ArticleId IdType="doi">10.1016/0378-1119(89)90120-0</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region><settlement><li>East Lansing</li></settlement><orgName><li>Université d'État du Michigan</li></orgName></list><tree><noCountry><name sortKey="Gan, Z R" sort="Gan, Z R" uniqKey="Gan Z" first="Z R" last="Gan">Z R Gan</name><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Yang, Y F" sort="Yang, Y F" uniqKey="Yang Y" first="Y F" last="Yang">Y F Yang</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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