Source:http://linkedlifedata.com/resource/pubmed/id/10852909
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rdf:type | |
lifeskim:mentions |
umls-concept:C0001271,
umls-concept:C0001478,
umls-concept:C0020792,
umls-concept:C0077404,
umls-concept:C1148926,
umls-concept:C1167622,
umls-concept:C1273518,
umls-concept:C1283195,
umls-concept:C1314939,
umls-concept:C1514562,
umls-concept:C1709915,
umls-concept:C1879547,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
36
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pubmed:dateCreated |
2000-10-13
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pubmed:abstractText |
The in vitro Ca(2+) regulation of the actomyosin Mg(2+)-ATPase at physiological ratios of actin, tropomyosin, and troponin occurs only in the presence of troponin T. We have previously demonstrated that a polypeptide corresponding to the first 191 amino acids of troponin T (TnT-(1-191)) activates the actomyosin Mg(2+)-ATPase in the presence of tropomyosin. In order to further characterize this activation domain, we constructed troponin T fragments corresponding to residues 1-157 (TnT-(1-157)), 1-76 (TnT-(1-76)), 77-157 (TnT-(77-157)), 77-191 (TnT-(77-191)), and 158-191 (TnT-(158-191)). Assays using these fragments demonstrated the following: (a) residues 1-76 do not bind to tropomyosin or actin; (b) residues 158-191 bind to actin cooperatively but not to tropomyosin; (c) the sequence 77-157 is necessary for troponin interaction with residue 263 of tropomyosin; (d) TnT-(77-191) on its own activates the actomyosin ATPase activity as described previously for TnT-(1-191). TnT-(1-157), TnT-(1-76), TnT-(77-157), TnT-(158-191), and combinations of TnT-(158-191) with TnT-(1-157) or TnT-(77-157) showed no effect on the ATPase activity. We conclude that the activation of actomyosin ATPase activity is mediated by a direct interaction between amino acids 77 and 191 of troponin T, tropomyosin, and actin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Ca(2 ) Mg(2 )-ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tropomyosin,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin T
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27513-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10852909-Actins,
pubmed-meshheading:10852909-Animals,
pubmed-meshheading:10852909-Binding Sites,
pubmed-meshheading:10852909-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:10852909-Calcium Signaling,
pubmed-meshheading:10852909-Chickens,
pubmed-meshheading:10852909-Circular Dichroism,
pubmed-meshheading:10852909-Enzyme Activation,
pubmed-meshheading:10852909-Kinetics,
pubmed-meshheading:10852909-Muscle, Skeletal,
pubmed-meshheading:10852909-Mutagenesis, Site-Directed,
pubmed-meshheading:10852909-Myosins,
pubmed-meshheading:10852909-Peptide Fragments,
pubmed-meshheading:10852909-Protein Conformation,
pubmed-meshheading:10852909-Recombinant Proteins,
pubmed-meshheading:10852909-Tropomyosin,
pubmed-meshheading:10852909-Troponin T
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pubmed:year |
2000
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pubmed:articleTitle |
Mapping the domain of troponin T responsible for the activation of actomyosin ATPase activity. Identification of residues involved in binding to actin.
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pubmed:affiliation |
Departamento de Bioquimica, Instituto de Quimica, Universidade de São Paulo CP 26.077, CEP 05599-970 São Paulo, Brazil.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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