Source:http://linkedlifedata.com/resource/pubmed/id/15752712
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2005-3-8
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pubmed:abstractText |
Ca(2+)-binding sites I and II in the N-terminal lobe of molluscan troponin C (TnC) have lost the ability to bind Ca(2+) due to substitutions of the amino acid residues responsible for Ca(2+) liganding. To evaluate the functional importance of the Ca(2+)-deficient N-terminal lobe in the Ca(2+)-regulatory function of molluscan troponin, we constructed chimeric TnCs comprising the N-terminal lobes from rabbit fast muscle and squid mantle muscle TnCs and the C-terminal lobe from akazara scallop TnC, TnC(RA), and TnC(SA), respectively. We characterized their biochemical properties as compared with those of akazara scallop wild-type TnC (TnC(AA)). According to equilibrium dialysis using (45)Ca(2+), TnC(RA), and TnC(SA) bound stoichiometrically 3 mol Ca(2+)/mol and 1 mol Ca(2+)/mol, respectively, as expected from their primary structures. All the chimeric TnCs exhibited difference-UV-absorption spectra at around 280-290 nm upon Ca(2+) binding and formed stable complexes with akazara scallop troponin I, even in the presence of 6M urea, if Ca(2+) was present. However, when the troponin complexes were constructed from chimeric TnCs and akazara scallop troponin T and troponin I, they showed different Ca(2+)-regulation abilities from each other depending on the TnC species. Thus, the troponin containing TnC(SA) conferred as high a Ca(2+) sensitivity to Mg-ATPase activity of rabbit actomyosin-akazara scallop tropomyosin as did the troponin containing TnC(AA), whereas the troponin containing TnC(RA) conferred virtually no Ca(2+) sensitivity. Our findings indicate that the N-terminal lobe of molluscan TnC plays important roles in molluscan troponin regulation, despite its inability to bind Ca(2+).
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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/Ca(2 ) Mg(2 )-ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Tropomyosin,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin C,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin I,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin T
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
436
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
83-90
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15752712-Animals,
pubmed-meshheading:15752712-Base Sequence,
pubmed-meshheading:15752712-Binding Sites,
pubmed-meshheading:15752712-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:15752712-Calcium,
pubmed-meshheading:15752712-Cations, Divalent,
pubmed-meshheading:15752712-Chimera,
pubmed-meshheading:15752712-Molecular Sequence Data,
pubmed-meshheading:15752712-Mollusca,
pubmed-meshheading:15752712-Mutation,
pubmed-meshheading:15752712-Peptides,
pubmed-meshheading:15752712-Rabbits,
pubmed-meshheading:15752712-Sequence Homology, Amino Acid,
pubmed-meshheading:15752712-Spectrophotometry, Ultraviolet,
pubmed-meshheading:15752712-Tropomyosin,
pubmed-meshheading:15752712-Troponin C,
pubmed-meshheading:15752712-Troponin I,
pubmed-meshheading:15752712-Troponin T
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pubmed:year |
2005
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pubmed:articleTitle |
Functional importance of Ca2+-deficient N-terminal lobe of molluscan troponin C in troponin regulation.
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pubmed:affiliation |
Laboratory of Biochemistry and Biotechnology, Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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