Mapping Contacts Between Regulatory Domains Of Skeletal Muscle Tnc And Tni By Analyses Of Single-chain Chimeras

dc.creatorTiroli A.O.
dc.creatorTasic L.
dc.creatorOliveira C.L.P.
dc.creatorBloch Jr. C.
dc.creatorTorriani I.
dc.creatorFarah C.S.
dc.creatorRamos C.H.I.
dc.date2005
dc.date2015-06-26T14:09:35Z
dc.date2015-11-26T14:09:35Z
dc.date2015-06-26T14:09:35Z
dc.date2015-11-26T14:09:35Z
dc.date.accessioned2018-03-28T21:10:09Z
dc.date.available2018-03-28T21:10:09Z
dc.identifier
dc.identifierFebs Journal. , v. 272, n. 3, p. 779 - 790, 2005.
dc.identifier1742464X
dc.identifier10.1111/j.1742-4658.2004.04515.x
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-13444253928&partnerID=40&md5=fd2a7e9290235d99781e2e7c1eec9968
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/93830
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/93830
dc.identifier2-s2.0-13444253928
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1241270
dc.descriptionThe troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnI-TnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 1-91 of TnC linked to residues 98-182 or 98-147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148-182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148-182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. On the other hand the TnI inhibitory and C-terminal domains were completely digested by trypsin in the absence of calcium while the addition of calcium results in the protection of only residues 114-137.
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dc.languageen
dc.publisher
dc.relationFEBS Journal
dc.rightsfechado
dc.sourceScopus
dc.titleMapping Contacts Between Regulatory Domains Of Skeletal Muscle Tnc And Tni By Analyses Of Single-chain Chimeras
dc.typeArtículos de revistas
dc.typeArtículos de revistas


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