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Article: Characterization of the human beta-crystallin gene Hu beta A3/A1 reveals ancestral relationships among the beta gamma-crystallin superfamily

TitleCharacterization of the human beta-crystallin gene Hu beta A3/A1 reveals ancestral relationships among the beta gamma-crystallin superfamily
Authors
Issue Date1986
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal of Biological Chemistry, 1986, v. 261 n. 26, p. 12420-12427 How to Cite?
AbstractWe report here the detailed structure of a human beta-crystallin gene, designated Hu beta A3/A1, which was isolated and characterized using homologous mouse and bovine beta-crystallin cDNAs. Hu beta A3/A1 consists of six exons, spanning approximately 8 kilobases. The first two exons code for an N-terminal extension of 32 amino acid residues, while the other four encode the four similar structural motifs of the predicted polypeptide. Sequence homologies among the latter four exons and their intron-exon junctions support a model of gene evolution based on two successive exon duplications. Transcription of Hu beta A3/A1 in the eye lens initiates 24 base pairs downstream of a putative TATA box and just 7 nucleotides upstream of a potential initiation codon, generating a single mRNA of approximately 1 kilobase. Comparison of Hu beta A3/A1 with the homologous bovine cDNA and the translation products of the corresponding bovine gene suggests that translation of Hu beta A3/A1 commences at either of two potential initiation codons located in the first and second exons. Differential use of these two codons predicts two polypeptides differing by the presence or absence of 17 amino acid residues at their N-termini.
Persistent Identifierhttp://hdl.handle.net/10722/44218
ISSN
2020 Impact Factor: 5.157
2023 SCImago Journal Rankings: 1.766
Other Identifiers
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorHogg, Den_HK
dc.contributor.authorTsui, L-Cen_HK
dc.contributor.authorGorin, Men_HK
dc.contributor.authorBreitman, MLen_HK
dc.date.accessioned2007-09-12T03:49:14Z-
dc.date.available2007-09-12T03:49:14Z-
dc.date.issued1986en_HK
dc.identifierhttp://www.jbc.org/cgi/reprint/261/26/12420.pdfen_HK
dc.identifier.citationJournal of Biological Chemistry, 1986, v. 261 n. 26, p. 12420-12427en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/44218-
dc.description.abstractWe report here the detailed structure of a human beta-crystallin gene, designated Hu beta A3/A1, which was isolated and characterized using homologous mouse and bovine beta-crystallin cDNAs. Hu beta A3/A1 consists of six exons, spanning approximately 8 kilobases. The first two exons code for an N-terminal extension of 32 amino acid residues, while the other four encode the four similar structural motifs of the predicted polypeptide. Sequence homologies among the latter four exons and their intron-exon junctions support a model of gene evolution based on two successive exon duplications. Transcription of Hu beta A3/A1 in the eye lens initiates 24 base pairs downstream of a putative TATA box and just 7 nucleotides upstream of a potential initiation codon, generating a single mRNA of approximately 1 kilobase. Comparison of Hu beta A3/A1 with the homologous bovine cDNA and the translation products of the corresponding bovine gene suggests that translation of Hu beta A3/A1 commences at either of two potential initiation codons located in the first and second exons. Differential use of these two codons predicts two polypeptides differing by the presence or absence of 17 amino acid residues at their N-termini.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistry-
dc.subject.meshAmino acid sequenceen_HK
dc.subject.meshCloning, molecularen_HK
dc.subject.meshCrystallins - geneticsen_HK
dc.subject.meshDna - analysisen_HK
dc.subject.meshGene expression regulationen_HK
dc.titleCharacterization of the human beta-crystallin gene Hu beta A3/A1 reveals ancestral relationships among the beta gamma-crystallin superfamilyen_HK
dc.typeArticleen_HK
dc.description.naturelink_to_OA_fulltexten_HK
dc.identifier.pmid3745196-
dc.identifier.scopuseid_2-s2.0-0023034960-
dc.identifier.volume261-
dc.identifier.issue26-
dc.identifier.spage12420-
dc.identifier.epage12427-
dc.identifier.isiWOS:A1986D999300078-
dc.identifier.issnl0021-9258-

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