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Registro Completo |
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
15/02/2005 |
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Data da última atualização: |
29/05/2018 |
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Autoria: |
TIROLI, A. O.; TASIC, L.; OLIVEIRA, C. L. P.; BLOCH JUNIOR, C.; TORRIANI, I.; FARAH, C. S.; RAMOS, C. H. I. |
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Título: |
Mapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras. |
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Ano de publicação: |
2005 |
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Fonte/Imprenta: |
The FEBS Journal, v. 272, n. 2, p. 779-790, 2005. |
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Idioma: |
Inglês |
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Conteúdo: |
The 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 TnITnC 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 191 of TnC linked to residues 98182 or 98147 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 148182, 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 (148182) 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 114137. MenosThe 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 TnITnC 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 191 of TnC linked to residues 98182 or 98147 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 148182, 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 (148182) 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. O... Mostrar Tudo |
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Palavras-Chave: |
Muscle. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/177877/1/ID-24788.pdf
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Marc: |
LEADER 02317naa a2200205 a 4500
001 1185506
005 2018-05-29
008 2005 bl uuuu u00u1 u #d
100 1 $aTIROLI, A. O.
245 $aMapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras.$h[electronic resource]
260 $c2005
520 $aThe 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 TnITnC 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 191 of TnC linked to residues 98182 or 98147 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 148182, 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 (148182) 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 114137.
653 $aMuscle
700 1 $aTASIC, L.
700 1 $aOLIVEIRA, C. L. P.
700 1 $aBLOCH JUNIOR, C.
700 1 $aTORRIANI, I.
700 1 $aFARAH, C. S.
700 1 $aRAMOS, C. H. I.
773 $tThe FEBS Journal$gv. 272, n. 2, p. 779-790, 2005.
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Registro original: |
Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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Registro Completo
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
23/08/2002 |
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Data da última atualização: |
03/10/2019 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
ANDRIOLI, A.; GOUVEIA, A. M. G.; ANDRADE, J. S.; PINHEIRO, R. R.; YORINORI, E. H.; SILVA, X. M. |
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Afiliação: |
ALICE ANDRIOLI, CNPC; RAIMUNDO RIZALDO PINHEIRO, CNPC. |
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Título: |
Diagnostic of the caprine arthritis encephalitis virus in uterine fluid and embryos of goats by virus isolation in cell culture and PCR nested. |
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Ano de publicação: |
2002 |
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Fonte/Imprenta: |
Theriogenology, Stoneham, v. 57, n. 1, p. 467, 2002. |
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Idioma: |
Inglês |
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Notas: |
Edição dos Proceedings Conference of the International Embryo Transfer Society, 2002, Foz do Iguassu, Paraná. Editado por: Mtthew B. Wheeler e Lawrence Smith. |
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Palavras-Chave: |
Artrite encefalite caprina. |
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Thesagro: |
Caprino; Diagnostico; Transferência de Embrião. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/36180/1/RAC-Diagnostic-of-the-caprine-arthritis-encephalitis.-.pdf
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Marc: |
LEADER 00877nam a2200217 a 4500
001 1528502
005 2019-10-03
008 2002 bl uuuu u00u1 u #d
100 1 $aANDRIOLI, A.
245 $aDiagnostic of the caprine arthritis encephalitis virus in uterine fluid and embryos of goats by virus isolation in cell culture and PCR nested.$h[electronic resource]
260 $aTheriogenology, Stoneham, v. 57, n. 1, p. 467$c2002
500 $aEdição dos Proceedings Conference of the International Embryo Transfer Society, 2002, Foz do Iguassu, Paraná. Editado por: Mtthew B. Wheeler e Lawrence Smith.
650 $aCaprino
650 $aDiagnostico
650 $aTransferência de Embrião
653 $aArtrite encefalite caprina
700 1 $aGOUVEIA, A. M. G.
700 1 $aANDRADE, J. S.
700 1 $aPINHEIRO, R. R.
700 1 $aYORINORI, E. H.
700 1 $aSILVA, X. M.
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Embrapa Caprinos e Ovinos (CNPC) |
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