scholarly journals Proton-magnetic-resonance studies on the interaction of rabbit skeletal-muscle troponin I with troponin C and actin

1982 ◽  
Vol 203 (1) ◽  
pp. 61-68 ◽  
Author(s):  
R J A Grand ◽  
B A Levine ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Specific Interaction ◽  
Troponin C ◽  
Terminal Region ◽  
Side Chains ◽  
Solution Structures ◽  
Arginine Residues ◽  
Cnbr Cleavage ◽  
Fast Twitch

1. The p.m.r. spectra of the larger CNBr-cleavage peptides of troponin I from rabbit fast-twitch skeletal muscle corresponded largely to those of fairly flexible solution structures. 2. On addition of troponin C to each of the CNBr-cleavage peptides in turn, perturbations of side chains were noted only for peptides CN5 (residues 1-21) and CN4 (residues 96-116). 3. In the presence of Ca2+, troponin C induced perturbations of the side chains of threonine-11, alanine, isoleucine and arginine residues of peptide CN5. 4. In the presence of Ca2+, troponin C induced perturbations of the side chains of phenylalanine, lysine and leucine residues of peptide CN4. 5. Irrespective of the presence or absence of Ca2+, specific interaction with actin was observed only with peptide CN4. In this case the side chains of arginine residues were perturbed. 6. It is concluded that actin interacts with the C-terminal region of peptide CN4, whereas troponin C interacts with the N-terminal region of peptide CN4 and with peptide CN5.

Fine Mapping of Five Human Skeletal Muscle Genes: Alpha-Tropomyosin, Beta-Tropomyosin, Troponin-I Slow-Twitch, Troponin-I Fast-Twitch, and Troponin-C Fast

1997 ◽  
Vol 230 (2) ◽  
pp. 347-350 ◽  
Author(s):  
Natascia Tiso ◽  
Luca Rampoldi ◽  
Alberto Pallavicini ◽  
Rosanna Zimbello ◽  
Davide Pandolfo ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Fine Mapping ◽  
Human Skeletal Muscle ◽  
Troponin I ◽  
Troponin C ◽  
Muscle Genes ◽  
Slow Twitch ◽  
Fast Twitch

scholarly journals Studies of the interaction of troponin I with proteins of the I-filament and calmodulin

1983 ◽  
Vol 209 (2) ◽  
pp. 417-426 ◽  
Author(s):  
A J G Moir ◽  
M Ordidge ◽  
R J A Grand ◽  
I P Trayer ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Troponin C ◽  
Sedimentation Equilibrium ◽  
Equilibrium Studies ◽  
Troponin Complex ◽  
Lysine Residues ◽  
C Complex ◽  
Modes Of Interaction ◽  
Fast Twitch

1. All lysine residues in native troponin I from rabbit fast-twitch skeletal muscle reacted with methyl acetimidate and ethyl acetimidate. 2. The reactivity of lysine-18 of troponin I to acetimidate was much diminished when the troponin I was complexed in the presence of Ca2+ with troponin C alone or in the whole troponin complex. 3. In the presence of EGTA, lysine-18 of troponin I in the troponin I-troponin C complex was more reactive to acetimidate than it was in the presence of Ca2+. 4. No masking of lysine residues could be detected when troponin I interacted with calmodulin or actin. 5. Sedimentation-equilibrium studies indicated that the complex of troponin I with calmodulin was more readily dissociated in the absence of Ca2+ than was its complex with troponin C under otherwise identical conditions. 6. These studies suggest that the nature of the involvement of the N-terminal region of troponin I is a major difference between its modes of interaction with calmodulin and with troponin C.

scholarly journals The complete amino acid sequence of chicken skeletal-muscle enolase

1986 ◽  
Vol 236 (1) ◽  
pp. 115-126 ◽  
Author(s):  
G A Russell ◽  
B Dunbar ◽  
L A Fothergill-Gilmore
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Peptide Bond ◽  
Peptide Bonds ◽  
Complete Amino Acid Sequence ◽  
Arginine Residues ◽  
Cnbr Cleavage ◽  
Yeast Enolase ◽  
Chicken Skeletal Muscle

The complete amino acid sequence of chicken skeletal-muscle enolase, comprising 433 residues, was determined. The sequence was deduced by automated sequencing of hydroxylamine-cleavage, CNBr-cleavage, o-iodosobenzoic acid-cleavage, clostripain-digest and staphylococcal-proteinase-digest fragments. The presence of several acid-labile peptide bonds and the tenacious aggregation of most CNBr-cleavage fragments meant that a commonly used sequencing strategy involving initial CNBr cleavage was unproductive. Cleavage at the single Asn-Gly peptide bond with hydroxylamine proved to be particularly useful. Comparison of the sequence of chicken enolase with the two yeast enolase isoenzyme sequences shows that the enzyme is strongly conserved, with 60% of the residues identical. The histidine and arginine residues implicated as being important for the activity of yeast enolase are conserved in the chicken enzyme. Secondary-structure predictions are analysed in an accompanying paper [Sawyer, Fothergill-Gilmore & Russell (1986) Biochem. J. 236, 127-130].

scholarly journals The cardiac-specific N-terminal region of troponin I positions the regulatory domain of troponin C

2014 ◽  
Vol 111 (40) ◽  
pp. 14412-14417 ◽  
Author(s):  
Peter M. Hwang ◽  
Fangze Cai ◽  
Sandra E. Pineda-Sanabria ◽  
David C. Corson ◽  
Brian D. Sykes
Keyword(s):  
Troponin I ◽  
Troponin C ◽  
Terminal Region ◽  
Regulatory Domain

scholarly journals Conformational modulation of slow skeletal muscle troponin T by an NH2-terminal metal-binding extension

2000 ◽  
Vol 279 (4) ◽  
pp. C1067-C1077 ◽  
Author(s):  
Jian-Ping Jin ◽  
Aihua Chen ◽  
Ozgur Ogut ◽  
Qi-Quan Huang
Keyword(s):  
Skeletal Muscle ◽  
Monoclonal Antibody ◽  
Metal Binding ◽  
Metal Ion ◽  
Troponin I ◽  
Troponin T ◽  
Terminal Region ◽  
Sequence Motif ◽  
Fast Skeletal Muscle ◽  
Slow Skeletal Muscle

Troponin T (TnT) is an essential element in the thin filament Ca2+-regulatory system controlling striated muscle contraction. Alternative RNA splicing generates developmental and muscle type-specific TnT isoforms differing in the hypervariable NH2-terminal region. Using avian fast skeletal muscle TnT containing a metal-binding segment, we have demonstrated a role of the NH2-terminal domain in modulating the conformation of TnT (Wang J and Jin JP. Biochemistry 37: 14519–14528, 1998). To further investigate the structure-function relationship of TnT, the present study constructed and characterized a recombinant protein in which the metal-binding peptide present in avian fast skeletal muscle TnT was fused to the NH2 terminus of mouse slow skeletal muscle TnT. Metal ion or monoclonal antibody binding to the NH2-terminal extension induced conformational changes in other domains of the model TnT molecule. This was shown by the altered affinity to a monoclonal antibody against the COOH-terminal region and a polyclonal antiserum recognizing multiple epitopes. Protein binding assays showed that metal binding to the NH2-terminal extension had effects on the interaction of TnT with troponin I, troponin C, and most significantly, tropomyosin. The data indicate that the NH2-terminal Tx [4–7 repeats of a sequence motif His-(Glu/Ala)-Glu-Ala-His] extension confers a specific conformational modulation in the slow skeletal muscle TnT.

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