Characterization of zero-length cross-links between rabbit skeletal muscle troponin C and troponin I: evidence for direct interaction between the inhibitory region of troponin I and the amino-terminal, regulatory domain of troponin C

Biochemistry ◽  
1990 ◽  
Vol 29 (1) ◽  
pp. 299-304 ◽  
Author(s):  
John Leszyk ◽  
Zenon Grabarek ◽  
John Gergely ◽  
John H. Collins
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Direct Interaction ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Regulatory Domain ◽  
Amino Terminal ◽  
Inhibitory Region ◽  
Cross Links

scholarly journals Troponin C-like proteins (calmodulins) from mammalian smooth muscle and other tissues

1979 ◽  
Vol 177 (2) ◽  
pp. 521-529 ◽  
Author(s):  
R J Grand ◽  
S V Perry ◽  
R A Weeks
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Troponin I ◽  
Smooth Muscles ◽  
Bovine Brain ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Polyacrylamide Gels ◽  
Rabbit Lung ◽  
Chicken Gizzard

1. An acidic protein with properties similar to those of troponin C from rabbit skeletal muscle has been shown to be present in bovine and rabbit smooth muscles, chicken gizzard and rabbit liver, kidney and lung. 2. A simple new method involving the use of organic solvents is described for the purification of the troponin C-like proteins from various tissues. 3. The troponin C-like proteins can be distinguished from rabbit skeletal-muscle toponin C by their electrophoretic behaviour on polyacrylamide gels at pH 8.3 in the presence and absence of Ca2+. The troponin C-like proteins have been shown to form complexes with rabbit skeletal-muscle troponin I that migrate on electrophoresis in polyacrylamide gels. 4. Behaviour on electrophoresis, amino acid analysis and the patterns of CNBr digests on polyacrylamide gels indicate that the troponin C-like proteins from bovine uterus and aorta, rabbit uterus, and liver and chicken gizzard are very similar to, if not identical with, bovine brain modulator protein. 5. With bovine cardiac muscle the organic-solvent method yields a preparation consisting of roughly similar amounts of troponin C and troponin C-like protein. 6. By the isotope-dilution technique, troponin C-like protein has been shown to represent 0.42% of the total protein in rabbit uterus. 7. In homogenates of smooth muscle, rabbit lung, kidney and brain, the troponin C-like proteins form a complex with other protein (or proteins) that requires Ca2+ for its formation and that is not dissociated in 9M-urea.

Residues 48 and 82 at the N-Terminal Hydrophobic Pocket of Rabbit Skeletal Muscle Troponin-C Photo-Cross-Link to Met121 of Troponin-I†

Biochemistry ◽  
1999 ◽  
Vol 38 (20) ◽  
pp. 6678-6688 ◽  
Author(s):  
Yin Luo ◽  
John Leszyk ◽  
Yude Qian ◽  
John Gergely ◽  
Terence Tao
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Cross Link ◽  
Hydrophobic Pocket

scholarly journals Characterization of a region of the primary sequence of troponin C involved in calcium ion-dependent interaction with troponin I

1978 ◽  
Vol 173 (2) ◽  
pp. 449-457 ◽  
Author(s):  
R A Weeks ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Gel Filtration ◽  
Troponin C ◽  
Fast Skeletal Muscle ◽  
Dependent Protein Kinase ◽  
Mechanism Of Interaction ◽  
Dependent Protein ◽  
Dependent Interaction

1. The CNBr digest of troponin C from rabbit fast skeletal muscle was shown to possess many of the functional properties of the whole troponin C molecule. 2. A peptide corresponding to residues 83-134 was isolated, which forms a Ca(2+-dependent complex with troponin I and neutralizes the inhibition by troponin I of the Mg(2+-stimulated adenosine triphosphatase of desensitized actomyosin. 3. The peptide inhibits the phosphorylation of fast-skeletal-muscle, but not cardiac-muscle, troponin I, by 3′ :5′-cyclic AMP-dependent protein kinase. In this property it was as effective as whole skeletal-muscle troponin C when compared on a molar basis. 4. Biological activity was also present in other fractions obtained from the CNBr digest. 5. By gel filtration and affinity chromatography of the whole CNBr digest of troponin C, two peptides, one of which was identified as representing residues 83-134, were shown to form Ca(2+-dependent complexes with troponin I. 6. The significance of these findings for the mechanism of interaction of troponin C and troponin I is discussed.

scholarly journals Production, crystallization, and preliminary X-ray analysis of rabbit skeletal muscle troponin complex consisting of troponin C and fragment (1-47) of troponin I

1997 ◽  
Vol 6 (4) ◽  
pp. 916-918 ◽  
Author(s):  
Yumiko Saijo ◽  
Soichi Takeda ◽  
Anna Scherer ◽  
Tomoyoshi Kobayashi ◽  
Yuichiro Maéda ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
X Ray ◽  
Troponin Complex
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