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Article: Structural and evolutionary relationships among five members of the human γ-crystallin gene family

TitleStructural and evolutionary relationships among five members of the human γ-crystallin gene family
Authors
Issue Date1985
PublisherAmerican Society for Microbiology.
Citation
Molecular And Cellular Biology, 1985, v. 5 n. 6, p. 1408-1414 How to Cite?
AbstractWe have characterized five human γ-crystallin genes isolated from a genomic phage library. DNA sequencing of four of the genes revealed that two of them predict polypeptides of 174 residues showing 71% homology in their amino acid sequence; the other two correspond to closely related pseudogenes which contain the same in-frame termination codon at identical positions in the coding sequence. Two of the genes and one of the pseudogenes are oriented in a head-to-tail fashion clustered within 22.5 kilobases. All three contain a TATA box 60 to 80 base pairs upstream of the initiation codon and a highly conserved segment of 44 base pairs in length immediately preceding the TATA box. The two genes and the two pseudogenes are similar in structure: each contains a small 5' exon encoding three amino acids followed by two larger exons that correspond exactly to the two similar structural domains of the polypeptide. The first intron varies from 100 to 110 base pairs, and the second intron ranges from 1 to several kilobases, rendering an overall gene size of 1.7 to 4.5 kilobases. At least one of the two pseudogenes appears to have been functional before inactivation, suggesting that their identical mutation was generated by gene conversion.
Persistent Identifierhttp://hdl.handle.net/10722/44210
ISSN
2015 Impact Factor: 4.427
2015 SCImago Journal Rankings: 3.806
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DC FieldValueLanguage
dc.contributor.authorMeakin, SOen_HK
dc.contributor.authorBreitman, MLen_HK
dc.contributor.authorTsui, LCen_HK
dc.date.accessioned2007-09-12T03:49:04Z-
dc.date.available2007-09-12T03:49:04Z-
dc.date.issued1985en_HK
dc.identifierhttp://mcb.asm.org/cgi/reprint/5/6/1408.pdfen_HK
dc.identifier.citationMolecular And Cellular Biology, 1985, v. 5 n. 6, p. 1408-1414en_HK
dc.identifier.issn0270-7306en_HK
dc.identifier.urihttp://hdl.handle.net/10722/44210-
dc.description.abstractWe have characterized five human γ-crystallin genes isolated from a genomic phage library. DNA sequencing of four of the genes revealed that two of them predict polypeptides of 174 residues showing 71% homology in their amino acid sequence; the other two correspond to closely related pseudogenes which contain the same in-frame termination codon at identical positions in the coding sequence. Two of the genes and one of the pseudogenes are oriented in a head-to-tail fashion clustered within 22.5 kilobases. All three contain a TATA box 60 to 80 base pairs upstream of the initiation codon and a highly conserved segment of 44 base pairs in length immediately preceding the TATA box. The two genes and the two pseudogenes are similar in structure: each contains a small 5' exon encoding three amino acids followed by two larger exons that correspond exactly to the two similar structural domains of the polypeptide. The first intron varies from 100 to 110 base pairs, and the second intron ranges from 1 to several kilobases, rendering an overall gene size of 1.7 to 4.5 kilobases. At least one of the two pseudogenes appears to have been functional before inactivation, suggesting that their identical mutation was generated by gene conversion.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Microbiology.en_HK
dc.relation.ispartofMolecular and Cellular Biologyen_HK
dc.rightsCopyright © American Society for Microbiology, Molecular and cellular biology, 1985, v. 5 n. 6, p. 1408-1414en_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshAmino acid sequenceen_HK
dc.subject.meshCloning, molecularen_HK
dc.subject.meshCrystallins - geneticsen_HK
dc.subject.meshDna, recombinant - analysisen_HK
dc.subject.meshGene conversionen_HK
dc.titleStructural and evolutionary relationships among five members of the human γ-crystallin gene familyen_HK
dc.typeArticleen_HK
dc.identifier.emailTsui, LC: tsuilc@hkucc.hku.hken_HK
dc.identifier.authorityTsui, LC=rp00058en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.pmid4033658-
dc.identifier.pmcidPMC366871-
dc.identifier.scopuseid_2-s2.0-0021957560en_HK
dc.identifier.volume5en_HK
dc.identifier.issue6en_HK
dc.identifier.spage1408en_HK
dc.identifier.epage1414en_HK
dc.identifier.isiWOS:A1985AJE9000026-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridMeakin, SO=7006735265en_HK
dc.identifier.scopusauthoridBreitman, ML=7005448008en_HK
dc.identifier.scopusauthoridTsui, LC=7102754167en_HK

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