Proximity Relationships between Residue 6 of Troponin I and Residues in Troponin C:  Further Evidence for Extended Conformation of Troponin C in the Troponin Complex†

Biochemistry ◽  
2000 ◽  
Vol 39 (50) ◽  
pp. 15306-15315 ◽  
Author(s):  
Yin Luo ◽  
John Leszyk ◽  
Bing Li ◽  
John Gergely ◽  
Terence Tao
Keyword(s):  
Troponin I ◽  
Troponin C ◽  
Extended Conformation ◽  
Troponin Complex

Troponin I Inhibitory Peptide (96−115) Has an Extended Conformation When Bound to Skeletal Muscle Troponin C†

Biochemistry ◽  
1999 ◽  
Vol 38 (21) ◽  
pp. 6911-6917 ◽  
Author(s):  
Griselda Hernández ◽  
Donald K. Blumenthal ◽  
Michael A. Kennedy ◽  
Clifford J. Unkefer ◽  
Jill Trewhella
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Troponin C ◽  
Inhibitory Peptide ◽  
Extended Conformation

scholarly journals Phosphorylation of troponin and the effects of interactions between the components of the complex

1974 ◽  
Vol 141 (3) ◽  
pp. 733-743 ◽  
Author(s):  
Samuel V. Perry ◽  
Heather A. Cole
Keyword(s):  
Protein Kinase ◽  
Troponin I ◽  
Troponin T ◽  
Troponin C ◽  
Phosphorylase Kinase ◽  
Significant Extent ◽  
Dependent Protein Kinase ◽  
Prolonged Incubation ◽  
Troponin Complex ◽  
Dependent Protein

1. The troponin complex from skeletal muscle contains approximately 1 mol of phosphate/80000g of complex, covalently bound to the troponin T component. 2. On prolonged incubation of the troponin complex or troponin T with phosphorylase kinase the phosphate content of troponin T was increased to approx. 3mol/mol. 3. On prolonged incubation of troponin I with phosphorylase kinase up to 1.6mol of phosphate/mol were incorporated. 4. Phosphorylation of troponin I was greatly inhibited by troponin C owing to the strong interaction between these proteins. Thus in the troponin complex troponin T was the main substrate for phosphorylase kinase. The phosphorylation of isolated troponin T was also inhibited by troponin C. 5. Troponin I was phosphorylated when the troponin complex was incubated with a bovine cardiac 3′:5′-cyclic AMP-dependent protein kinase. Troponin T either in its isolated form or in the troponin complex was not phosphorylated by bovine protein kinase to any significant extent under the conditions used. 6. If the troponin complex was dephosphorylated to 0.2mol/mol, or phosphorylated up to 2.5mol/mol there was no significant effect on the ability of normal concentrations to confer Ca2+sensitivity on the adenosine triphosphatase of densensitized actomyosin.

scholarly journals Structure of the troponin complex. Implications of photocross-linking of troponin I to troponin C thiol mutants.

1994 ◽  
Vol 269 (8) ◽  
pp. 5725-5729
Author(s):  
T. Kobayashi ◽  
T. Tao ◽  
J. Gergely ◽  
J.H. Collins
Keyword(s):  
Troponin I ◽  
Troponin C ◽  
Troponin Complex

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 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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