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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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 | Acesso ao texto completo restrito à biblioteca da Embrapa Mandioca e Fruticultura. Para informações adicionais entre em contato com cnpmf.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Mandioca e Fruticultura. |
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Data corrente: |
13/12/2011 |
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Data da última atualização: |
01/11/2013 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
SEREJO, J. A. dos S.; SOARES, T. L.; SOUZA, A. da S.; COSTA, M. A. P. C. |
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Afiliação: |
JANAY ALMEIDA DOS SANTOS SEREJO, CNPMF; TALIANE LEILA SOARES, UFRB; ANTONIO DA SILVA SOUZA, CNPMF; MARIA ANGÉLICA PEREIRA DE CARVALHO COSTA, UFRB. |
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Título: |
Influence of floral tissue extracts on in vitro pollen germination and pollen tube growth in banana. |
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Ano de publicação: |
2011 |
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Fonte/Imprenta: |
In: PROMUSA SYMPOSIUM, 2011, Salvador. Bananas and plantains: toward sustainable global production and improved uses: abstracts. [Montepellier.]: [Bioversity International, 2011. p. 137-138. |
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Idioma: |
Inglês |
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Conteúdo: |
The genetic breeding of banana through hybridization is limited by the occurrence of sterility in most cultivars resulting in low production or absence of seeds. Studies are needed to better understand the processes involved in banana sterility and to develop strategies to overcome this barrier. |
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Palavras-Chave: |
Musa spp. |
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Thesagro: |
Banana. |
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Thesaurus NAL: |
breeding; stigma. |
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Categoria do assunto: |
G Melhoramento Genético |
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Marc: |
LEADER 00995nam a2200193 a 4500
001 1909456
005 2013-11-01
008 2011 bl uuuu u00u1 u #d
100 1 $aSEREJO, J. A. dos S.
245 $aInfluence of floral tissue extracts on in vitro pollen germination and pollen tube growth in banana.
260 $aIn: PROMUSA SYMPOSIUM, 2011, Salvador. Bananas and plantains: toward sustainable global production and improved uses: abstracts. [Montepellier.]: [Bioversity International, 2011. p. 137-138.$c2011
520 $aThe genetic breeding of banana through hybridization is limited by the occurrence of sterility in most cultivars resulting in low production or absence of seeds. Studies are needed to better understand the processes involved in banana sterility and to develop strategies to overcome this barrier.
650 $abreeding
650 $astigma
650 $aBanana
653 $aMusa spp
700 1 $aSOARES, T. L.
700 1 $aSOUZA, A. da S.
700 1 $aCOSTA, M. A. P. C.
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Embrapa Mandioca e Fruticultura (CNPMF) |
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