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dc.contributor.authorChandra, Murali-
dc.contributor.authorDa Silva, Elizabeth Fidalgo-
dc.contributor.authorSorenson, Martha M.-
dc.contributor.authorFerro, Jesus A.-
dc.contributor.authorPearlstone, Joyce R.-
dc.contributor.authorNash, Bruce E.-
dc.contributor.authorBorgford, Thor-
dc.contributor.authorKay, Cyril M.-
dc.contributor.authorSmillie, Lawrence B.-
dc.date.accessioned2014-05-27T11:17:56Z-
dc.date.accessioned2016-10-25T18:13:19Z-
dc.date.available2014-05-27T11:17:56Z-
dc.date.available2016-10-25T18:13:19Z-
dc.date.issued1994-05-27-
dc.identifierhttp://www.jbc.org/content/269/21/14988.long-
dc.identifier.citationJournal of Biological Chemistry, v. 269, n. 21, p. 14988-14994, 1994.-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/11449/64480-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/64480-
dc.description.abstractTo assess the structural and functional significance of the N helix (residues 3-13) of avian recombinant troponin C (rTnC), we have constructed NHdel, in which residues 1-11 have been deleted, both in rTnC and in the spectral probe mutant F29W (Pearlstone, J. R., Borgford, T., Chandra, M., Oikawa, K., Kay, C. M., Herzberg, O., Moult, J., Herklotz, A., Reinach, F. C., and Smillie, L.B. (1992) Biochemistry 31, 6545-6553). Comparison of the far- and near-UV CD spectra (±Ca2+) of F29W and F29W/ NHdel and titration of the Ca2+-induced ellipticity and fluorescence changes indicates that the deletion has little effect on the global fold of the molecule but reduces the Ca2+ affinity of the N domain, but not the C domain, by 1.6-1.8-fold. Comparisons of the mutants NHdel, F29W, and F29W/NHdel with rTnC have been made using several functional assays. In reconstituted troponin-tropomyosin actomyosin subfragment 1 and myofibrillar ATPase systems, both F29W and NHdel have significantly reduced Ca2+-activated enzymic activities. These effects are cumulative in the double mutant F29W/ NHdel. On the other hand, maximal isometric tension development in Ca2+-activated reconstituted skinned fibers is not affected with F29W and NHdel, although the Ca2+ sensitivity of NHdel in this system is markedly reduced. We conclude that both mutations, NHdel and F29W, are functionally deleterious, possibly affecting interactions of the N domain with troponin I and/or T.en
dc.format.extent14988-14994-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectAves-
dc.subjectGallus gallus-
dc.subjectadenosine triphosphatase-
dc.subjectcalcium ion-
dc.subjectcalmodulin-
dc.subjectmuscle protein-
dc.subjectmyosin adenosine triphosphatase-
dc.subjecttropomyosin-
dc.subjecttroponin c-
dc.subjectanimal cell-
dc.subjectanimal tissue-
dc.subjectbinding affinity-
dc.subjectchicken-
dc.subjectdeletion mutant-
dc.subjectgene deletion-
dc.subjectnonhuman-
dc.subjectpriority journal-
dc.subjectprotein analysis-
dc.subjectprotein domain-
dc.subjectprotein structure-
dc.subjectskeletal muscle-
dc.subjectstructure activity relation-
dc.subjectAnimal-
dc.subjectBase Sequence-
dc.subjectBinding Sites-
dc.subjectCalcium-
dc.subjectChickens-
dc.subjectCircular Dichroism-
dc.subjectMolecular Sequence Data-
dc.subjectMuscles-
dc.subjectMutagenesis, Site-Directed-
dc.subjectOligodeoxyribonucleotides-
dc.subjectPeptide Fragments-
dc.subjectSequence Deletion-
dc.subjectSpectrophotometry, Ultraviolet-
dc.subjectSupport, Non-U.S. Gov't-
dc.subjectTroponin-
dc.subjectTroponin C-
dc.titleThe Effects of N Helix Deletion and Mutant F29W on the Ca2+ Binding and Functional Properties of Chicken Skeletal Muscle Troponin Cen
dc.typeoutro-
dc.contributor.institutionUniversity of Alberta-
dc.contributor.institutionUniv. Federal de Rio de Janeiro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionSimon Fraser University-
dc.description.affiliationMed. Res. Cncl. Canada Grp. P. Department of Biochemistry University of Alberta, Edmonton, Alta. T6G 2H7-
dc.description.affiliationDepto. de Bioquimica Médica ICB Univ. Federal de Rio de Janeiro, 21941-590 Rio de Janeiro, RJ-
dc.description.affiliationDept. de Tecnologia Universidade Estadual Paulista, CEP 14870, Jaboticabal, Sao Paulo-
dc.description.affiliationDept. of Chemistry Inst. of Molec. Biol. and Biochem. Simon Fraser University, Burnaby, BC V5A 1S6-
dc.description.affiliationUnespDept. de Tecnologia Universidade Estadual Paulista, CEP 14870, Jaboticabal, Sao Paulo-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofJournal of Biological Chemistry-
dc.identifier.scopus2-s2.0-0028362401-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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