Ca2+, Mg2+, and Troponin I Inhibitory Peptide Binding to a Phe-154 to Trp Mutant of Chicken Skeletal Muscle Troponin C

Biochemistry ◽  
1994 ◽  
Vol 33 (10) ◽  
pp. 2961-2969 ◽  
Author(s):  
Murali Chandra ◽  
William D. McCubbin ◽  
Kim Oikawa ◽  
Cyril M. Kay ◽  
Lawrence B. Smillie
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Peptide Binding ◽  
Troponin C ◽  
Inhibitory Peptide ◽  
Trp Mutant ◽  
Chicken Skeletal Muscle

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

Calmodulin and troponin C: affinity chromatographic study of divalent cation requirements for troponin I inhibitory peptide (residues 104–115), mastoparan, and fluphenazine binding

1987 ◽  
Vol 65 (11) ◽  
pp. 982-988 ◽  
Author(s):  
Jennifer E. Van Eyk ◽  
Robert S. Hodges
Keyword(s):  
Troponin I ◽  
Troponin C ◽  
Homologous Region ◽  
Affinity Column ◽  
Chromatographic Study ◽  
Inhibitory Peptide ◽  
Receptor Sites ◽  
Inhibitory Region ◽  
Correct Alignment ◽  
Correct Structure

The different conformations induced by the binding of Mg2+ or Ca2+ to troponin C (TnC) and calmodulin (CaM) results in the exposure of various interfaces with potential to bind target compounds. The interaction of TnC or CaM with three affinity columns with ligands of either the synthetic peptide of troponin I (TnI) inhibitory region (residues 104–115), mastoparan (a wasp venom peptide), or fluphenazine (a phenothiazine drug) were investigated in the presence of Mg2+ or Ca2+. TnC and CaM in the presence of either Ca2+ or Mg2+ bound to the TnI peptide 104–115. The cation specificity for this interaction firmly establishes that the TnI inhibitory region binds to the high affinity sites of TnC (most likely the N-terminal helix of site III) and presumably the homologous region of CaM. Mastoparan interacted strongly with both proteins in the presence of Ca2+ but, in the presence of Mg2+, did not bind to TnC and only bound weakly to CaM. Fluphenazine bound to TnC and CaM only in the presence of Ca2+. When the ligands interacted with either proteins there was an increase in cation affinity, such that TnC and CaM were eluted from the TnI peptide or mastoparan affinity column with 0.1 M EDTA compared with the 0.01 M EDTA required to elute the proteins from the fluphenazine column. The interaction of these ligands with their receptor sites on TnC and CaM require a specific and spatially correct alignment of hydrophobic and negatively charged residues on these proteins. In the case of the TnI peptide, which represents a naturally occurring target protein for TnC, Mg2+ and Ca2+ can induce the correct structure in TnC or CaM for interaction, while only Ca2+ can induce the correct structure for mastoparan or fluophenazine binding.

scholarly journals Cloning and expression of chicken skeletal muscle troponin I inEscherichia coli: The role of rare codons on the expression level

1993 ◽  
Vol 2 (6) ◽  
pp. 1053-1056 ◽  
Author(s):  
Ronaldo B. Quaggio ◽  
Jesus A. Ferro ◽  
Patricia B. Monteiro ◽  
Fernando C. Reinach
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Cloning And Expression ◽  
Expression Level ◽  
Inescherichia Coli ◽  
Rare Codons ◽  
Chicken Skeletal Muscle

Cardiac troponin I inhibitory peptide: location of interaction sites on troponin C

FEBS Letters ◽  
2000 ◽  
Vol 469 (2-3) ◽  
pp. 168-172 ◽  
Author(s):  
M.Bret Abbott ◽  
Alex Dvoretsky ◽  
Vadim Gaponenko ◽  
Paul R Rosevear
Keyword(s):  
Cardiac Troponin ◽  
Troponin I ◽  
Troponin C ◽  
Cardiac Troponin I ◽  
Inhibitory Peptide ◽  
Interaction Sites

Structure of chicken skeletal muscle troponin C at 1.78 Å resolution

1994 ◽  
Vol 50 (1) ◽  
pp. 40-49 ◽  
Author(s):  
K. A. Satyshur ◽  
D. Pyzalska ◽  
M. Greaser ◽  
S. T. Rao ◽  
M. Sundaralingam
Keyword(s):  
Skeletal Muscle ◽  
Troponin C ◽  
Chicken Skeletal Muscle

scholarly journals Immunohistochemical and ultrastructural distribution of antibodies to troponin-C and troponin-I in normal and dystrophic chicken skeletal muscle.

1978 ◽  
Vol 26 (4) ◽  
pp. 258-266 ◽  
Author(s):  
F J Wilson ◽  
D Camiscoli ◽  
M J Irish ◽  
T Hirabayashi
Keyword(s):  
Troponin I ◽  
Pectoral Muscle ◽  
Troponin C ◽  
Dystrophic Muscle ◽  
Ultrastructural Studies ◽  
Antigenic Sites ◽  
Immuno Electron Microscopy ◽  
And Control ◽  
Chicken Skeletal Muscle ◽  
Dystrophic Chicken

The pectoral muscles from normal and dystrophic chickens were reacted with rabbit antisera to troponin-C and to troponin-I, and the distribution of antibodies was determined by fluorescence microscopy of antibody-stained myofibrils and immuno-electron microscopy of separated I band segments. Chickens of dystrophic strain 308 and control New Hampshire hens were used in this work. Myofibrils which were prepared from both normal and dystrophic muscles and reacted with anti-troponin-I were fluorescent in the I band and A band regions. The Z lines and H zones were unstained. Myofibrils prepared from normal pectoral muscle and treated with anti-troponin-C yielded a pattern of fluorescence similar to that for anti-troponin-I treated myofibrils. However, those myofibrils isolated from dystrophic muscle and reacted with anti-tropinin-C had a weak fluorescence over their entire lengths, and discrete A- and I-band staining was not visible. These results were confirmed by ultrastructural studies of separated I segments reacted with the antisera. It is concluded that in the dystrophic muscle either the antigenic sites of troponin-C are changed which results in a loss of antibody-combining ability or these sites are masked in some way which prevents the reaction with the antibody.

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