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Article: Sequence analysis and chromosomal localization of human cap Z. Conserved residues within the actin-binding domain may link cap Z to gelsolin/severin and profilin protein families

TitleSequence analysis and chromosomal localization of human cap Z. Conserved residues within the actin-binding domain may link cap Z to gelsolin/severin and profilin protein families
Authors
Issue Date1995
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, 1995, v. 270 n. 37, p. 21472-21479 How to Cite?
AbstractFrom a human retinal cDNA library, we have isolated cDNAs that are homologs for the α2 and β subunits of chicken Cap Z. The derived human α subunit shares 95% amino acid identity with the chicken α2 subunit; the β subunit is 99% identical to the chicken subunit residues 1-243. The remaining portion of the human β subunit (244-272) diverges significantly with only 8 out of 29 C-terminal amino acids conserved between the two species. This lack of conservation is of particular interest because the chicken C terminus contains an actin-binding domain. Cosedimentation assays with F-actin show that human Cap Z binds actin with an affinity equal that of chicken Cap Z. These results point to the eight shared amino acids as critical for actin binding, three of which are regularly spaced leucines. These apolar residues and one outside the region of divergence align well with those residues of the actin-binding α-helix proposed for gelsolin segment 1. The apolar residues as well as three polar amino acids are also conserved in other capping, capping and severing, and monomer-binding proteins. Amino acid substitutions in the chicken β subunit of the two most highly conserved leucines result in significant decreases in F-actin binding activity. The human α2 gene (CAPZA2) has been mapped to chromosome 7 position q31.2-q31.3 and the β gene (CAPZB) to chromosome 1 region p36.1.
Persistent Identifierhttp://hdl.handle.net/10722/44287
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBarronCasella, EAen_HK
dc.contributor.authorTorres, MAen_HK
dc.contributor.authorScherer, SWen_HK
dc.contributor.authorHeng, HHQen_HK
dc.contributor.authorTsui , LCen_HK
dc.contributor.authorCasella, JFen_HK
dc.date.accessioned2007-09-12T03:50:41Z-
dc.date.available2007-09-12T03:50:41Z-
dc.date.issued1995en_HK
dc.identifier.citationJournal Of Biological Chemistry, 1995, v. 270 n. 37, p. 21472-21479en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/44287-
dc.description.abstractFrom a human retinal cDNA library, we have isolated cDNAs that are homologs for the α2 and β subunits of chicken Cap Z. The derived human α subunit shares 95% amino acid identity with the chicken α2 subunit; the β subunit is 99% identical to the chicken subunit residues 1-243. The remaining portion of the human β subunit (244-272) diverges significantly with only 8 out of 29 C-terminal amino acids conserved between the two species. This lack of conservation is of particular interest because the chicken C terminus contains an actin-binding domain. Cosedimentation assays with F-actin show that human Cap Z binds actin with an affinity equal that of chicken Cap Z. These results point to the eight shared amino acids as critical for actin binding, three of which are regularly spaced leucines. These apolar residues and one outside the region of divergence align well with those residues of the actin-binding α-helix proposed for gelsolin segment 1. The apolar residues as well as three polar amino acids are also conserved in other capping, capping and severing, and monomer-binding proteins. Amino acid substitutions in the chicken β subunit of the two most highly conserved leucines result in significant decreases in F-actin binding activity. The human α2 gene (CAPZA2) has been mapped to chromosome 7 position q31.2-q31.3 and the β gene (CAPZB) to chromosome 1 region p36.1.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 Chemistryen_HK
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.subject.meshCaenorhabditis elegans - metabolismen_HK
dc.subject.meshChromosomes, human, pair 1en_HK
dc.subject.meshChromosomes, human, pair 7en_HK
dc.subject.meshHominidae - geneticsen_HK
dc.subject.meshMicrofilament proteinsen_HK
dc.titleSequence analysis and chromosomal localization of human cap Z. Conserved residues within the actin-binding domain may link cap Z to gelsolin/severin and profilin protein familiesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=270&issue=37&spage=21472&epage=21479&date=1995&atitle=Sequence+analysis+and+chromosomal+localization+of+human+Cap+Z.+Conserved+residues+within+the+actin-binding+domain+may+link+Cap+Z+to+gelsolin/severin+and+profilin+protein+familiesen_HK
dc.identifier.emailTsui , LC: tsuilc@hkucc.hku.hken_HK
dc.identifier.authorityTsui , LC=rp00058en_HK
dc.description.naturelink_to_OA_fulltexten_HK
dc.identifier.doi10.1074/jbc.270.37.21472en_HK
dc.identifier.pmid7665558-
dc.identifier.scopuseid_2-s2.0-0029132690en_HK
dc.identifier.volume270en_HK
dc.identifier.issue37en_HK
dc.identifier.spage21472en_HK
dc.identifier.epage21479en_HK
dc.identifier.isiWOS:A1995RU75700012-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridBarronCasella, EA=6602442318en_HK
dc.identifier.scopusauthoridTorres, MA=7402581262en_HK
dc.identifier.scopusauthoridScherer, SW=35374654500en_HK
dc.identifier.scopusauthoridHeng, HHQ=7005338076en_HK
dc.identifier.scopusauthoridTsui , LC=7102754167en_HK
dc.identifier.scopusauthoridCasella, JF=7003988050en_HK

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