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Article: A base substitution in the exon of a collagen gene causes alternative splicing and generates a structurally abnormal polypeptide in a patient with Ehlers-Danlos Syndrome Type VII

TitleA base substitution in the exon of a collagen gene causes alternative splicing and generates a structurally abnormal polypeptide in a patient with Ehlers-Danlos Syndrome Type VII
Authors
Issue Date1989
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/emboj/index.html
Citation
Embo Journal, 1989, v. 8 n. 6, p. 1705-1710 How to Cite?
AbstractAn unusual splicing mutation has been characterized in the pro α1(I) collagen gene of a sporadic case of Ehlers-Danlos Syndrome Type VII. Cloning of primer extended cDNA in conjunction with R-looping experiments established that nearly half of the pro α1(I) collagen gene transcripts are abnormally spliced, for they lack exon 6 sequences. Analysis of cloned genomic fragments revealed that one of the proband's alleles displays the substitution of an A for a G in the last nucleotide of exon 6. The change converts the normal Met (ATG) codon to Ile (ATA) and, in addition, obliterates a NcoI restriction site. The latter event was exploited to demonstrate the de novo nature of the muation since DNA from the unaffected parents was fully digested with the enzyme, after in vitro amplification by the polymerase chain reaction. Further confirmation of the missplicing was obtained by transient expression into animal cells of allelic minigene constructs. Finally, Western blot analysis of cyanogen bromide cleaved collagen and nucleotide sequencing of appropriately selected cDNA clones demonstrated the production of relatively low amounts of correctly spliced molecules harboring the Ile substitution, as well.
Persistent Identifierhttp://hdl.handle.net/10722/147339
ISSN
2015 Impact Factor: 9.643
2015 SCImago Journal Rankings: 7.450
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWeil, Den_US
dc.contributor.authorD'alessio, Men_US
dc.contributor.authorRamirez, Fen_US
dc.contributor.authorDe Wet, Wen_US
dc.contributor.authorCole, WGen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorBateman, JFen_US
dc.date.accessioned2012-05-29T06:03:02Z-
dc.date.available2012-05-29T06:03:02Z-
dc.date.issued1989en_US
dc.identifier.citationEmbo Journal, 1989, v. 8 n. 6, p. 1705-1710en_US
dc.identifier.issn0261-4189en_US
dc.identifier.urihttp://hdl.handle.net/10722/147339-
dc.description.abstractAn unusual splicing mutation has been characterized in the pro α1(I) collagen gene of a sporadic case of Ehlers-Danlos Syndrome Type VII. Cloning of primer extended cDNA in conjunction with R-looping experiments established that nearly half of the pro α1(I) collagen gene transcripts are abnormally spliced, for they lack exon 6 sequences. Analysis of cloned genomic fragments revealed that one of the proband's alleles displays the substitution of an A for a G in the last nucleotide of exon 6. The change converts the normal Met (ATG) codon to Ile (ATA) and, in addition, obliterates a NcoI restriction site. The latter event was exploited to demonstrate the de novo nature of the muation since DNA from the unaffected parents was fully digested with the enzyme, after in vitro amplification by the polymerase chain reaction. Further confirmation of the missplicing was obtained by transient expression into animal cells of allelic minigene constructs. Finally, Western blot analysis of cyanogen bromide cleaved collagen and nucleotide sequencing of appropriately selected cDNA clones demonstrated the production of relatively low amounts of correctly spliced molecules harboring the Ile substitution, as well.en_US
dc.languageengen_US
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/emboj/index.htmlen_US
dc.relation.ispartofEMBO Journalen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshDna - Geneticsen_US
dc.subject.meshEhlers-Danlos Syndrome - Classification - Geneticsen_US
dc.subject.meshExonsen_US
dc.subject.meshHumansen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMutationen_US
dc.subject.meshProcollagen - Geneticsen_US
dc.subject.meshRna Splicingen_US
dc.titleA base substitution in the exon of a collagen gene causes alternative splicing and generates a structurally abnormal polypeptide in a patient with Ehlers-Danlos Syndrome Type VIIen_US
dc.typeArticleen_US
dc.identifier.emailChan, D:chand@hkucc.hku.hken_US
dc.identifier.authorityChan, D=rp00540en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid2767050en_US
dc.identifier.scopuseid_2-s2.0-0024446126en_US
dc.identifier.volume8en_US
dc.identifier.issue6en_US
dc.identifier.spage1705en_US
dc.identifier.epage1710en_US
dc.identifier.isiWOS:A1989U846900010-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridWeil, D=7103234861en_US
dc.identifier.scopusauthoridD'Alessio, M=7004168029en_US
dc.identifier.scopusauthoridRamirez, F=7202326091en_US
dc.identifier.scopusauthoridDe Wet, W=6603768380en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US

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