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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
49
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pubmed:dateCreated |
1996-1-25
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pubmed:abstractText |
Mild proteolytic cleavage of the troponin complex yields TnT1, the N-terminal fragment of troponin T, and TnT2IC, a complex of the C-terminal fragment of troponin T (TnT2) with troponin I (TnI) and troponin C (TnC) [Morris, E. P., & Lehrer, S. S. (1984) Biochemistry 23, 2214-2220]. Both TnT1 and TnT2IC bind tightly to the tropomyosin.actin (Tm.actin) thin filament and influence the interaction of myosin subfragment 1 (S1) with Tm.actin. TnT1 does not affect the rate of S1 binding to Tm.actin but does increase the cooperativity with which S1 "turns on" Tm.actin, monitored by the excimer fluorescence of a pyrene label attached to Cys 190 of Tm [Geeves, M.A., & Lehrer, S. S. (1994) Biophys. J. 67, 273-282]. The apparent cooperative unit size of Tm.actin is increased from 6 to 9 by TnT1 and to 12 by whole troponin. In contrast, TnT2IC has no effect on the cooperativity of Tm.actin but does make the apparent S1-binding rate constant, kapp, Ca(2+)-sensitive; i.e., in the absence of Ca2+, kapp is reduced 2-3-fold by both TnT2IC and whole troponin. Thus, the N- and C-terminal regions of TnT appear to act independently in modulating effects of S1 binding to the Tm.actin thin filament that are important in regulation.
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pubmed:grant | |
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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Subfragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin T
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15890-4
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8519745-Actins,
pubmed-meshheading:8519745-Adenosine Triphosphate,
pubmed-meshheading:8519745-Animals,
pubmed-meshheading:8519745-Calcium,
pubmed-meshheading:8519745-Kinetics,
pubmed-meshheading:8519745-Muscle, Skeletal,
pubmed-meshheading:8519745-Myosin Subfragments,
pubmed-meshheading:8519745-Peptide Fragments,
pubmed-meshheading:8519745-Protein Binding,
pubmed-meshheading:8519745-Rabbits,
pubmed-meshheading:8519745-Time Factors,
pubmed-meshheading:8519745-Troponin,
pubmed-meshheading:8519745-Troponin T
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pubmed:year |
1995
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pubmed:articleTitle |
Separation and characterization of the two functional regions of troponin involved in muscle thin filament regulation.
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pubmed:affiliation |
Max Planck Institute für Molekulare Physiologie, Dortmund, Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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