Localization and Mode of Action of the Inhibitory Protein Component of the Troponin Complex

Perry, S. V.; Cole, Heather; Head, James F.; Wilson, Frank J.

doi:10.1101/sqb.1973.037.01.035

Cited by 99 publications

(53 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…1). In both cases neutralisation of the inhibition was complete when the molar ratio of troponin C or modulator protein to troponin I was about 0.5 [22].…”

Section: Resultsmentioning

confidence: 90%

See 1 more Smart Citation

Effect of the troponin C‐like protein from bovine brain (brain modulator protein) on the Mg²⁺‐stimulated ATPase of skeletal muscle actomyosin

1976

View full text Add to dashboard Cite

“…1). In both cases neutralisation of the inhibition was complete when the molar ratio of troponin C or modulator protein to troponin I was about 0.5 [22].…”

Section: Resultsmentioning

confidence: 90%

“…At lower molar ratios of skeletal troponin C to troponin I, some Ca*+-sensitivity of the ATPase was observed [22] , although it was not complete and disappeared at higher ratios (fig. la).…”

Section: Resultsmentioning

confidence: 99%

Effect of the troponin C‐like protein from bovine brain (brain modulator protein) on the Mg²⁺‐stimulated ATPase of skeletal muscle actomyosin

1976

View full text Add to dashboard Cite

“…The inhibition of the actomyosin ATPase is neutralized when calcium-saturated TnC forms a complex with TnI (Perry et al, 1972;Weeks & Perry, 1978;Chong et al, 1983). This calcium-dependent interaction between TnC and TnI is one of the key processes in the regulation of contraction in skeletal muscle and thus is important to the understanding of the mechanism of muscle contraction on a molecular level (for recent reviews, see Leavis & Gergely, 1984;Zot & Potter, 1987).…”

Section: ;mentioning

confidence: 99%

A ¹H NMR study of a ternary peptide complex that mimics the interaction between troponin C and troponin I

et al. 1992

View full text Add to dashboard Cite

The troponin I peptide Na-acetyl TnI Abbreviations: s-TnC, skeletal troponin C; TnI, troponin I; TnT, troponin T; CaM, calmodulin; SCIII, Ac-(AlOl) (Y112) s-TnC (93-126) amide; SCIV, Ac-s-TnC (129-162) amide; TnIp, Na-acetyl TnI (104-115) amide; TR2C, C-terminal domain (residues 92-162) of s-TnC; NOE, nuclear Overhauser enhancement; TRNOE, transferred nuclear Overhauser enhancement; 2D NOESY, two-dimensional nuclear Overhauser enhancement spectroscopy; 2D DQF-COSY, two-dimensional double-quantum filtered correlation spectroscopy; TOCSY, total correlation spectroscopy; DSS, 2,2"dimethyl-2-silapentane-5-sulfonate; DTT, dithiothreitol; SDS, sodium dodecyl sulfate; PAGE, polyacrylamide gel electrophoresis.

show abstract

“…It has long been appreciated that in inhibitory proteins such as troponin I and caldesmon inhibitory function is related to concentrations of positive charge (the inhibitory peptide of troponin I, residues 104 -115, contains 4 arginines and 2 lysines (40,41)). There are complementary clusters of negative charged amino acids on the surface of actin, the most notable of which is at the bottom of domain 2 (Asp 56 , Glu 57 , Glu 93 ).…”

Section: Glu 93mentioning

confidence: 99%

Tropomyosin and Troponin Regulation of Wild Type and E93K Mutant Actin Filaments from Drosophila Flight Muscle

Bing¹,

Razzaq²,

Sparrow³

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

In the Drosophila flight muscle actin mutant E93K there is a charge reversal on the surface of actin close to the proposed position of tropomyosin when it is in the off state. Using a quantitative in vitro motility assay we have found that the wild type Drosophila ACT88F actin behaved like rabbit skeletal muscle actin when tropomyosin and troponin were added at pCa5 and pCa9. In contrast the effect of tropomyosin upon the E93K mutant actin filament movement was completely different from wild type and resembled the response of wild type with tropomyosin؉troponin at pCa9 (i.e. the filaments were switched off). Velocity of E93K actin did not increase, and the fraction of filaments motile was reduced to less than 15% by adding up to 30 nM tropomyosin. When myosin subfragment-1 modified by N-ethylmaleimide was mixed with mutant E93K actin-tropomyosin filaments we observed that it restored motility of the filaments to the level observed with E93K actin alone. We conclude that electrostatic charge on the surface of domain 2 of actin plays a critical role in determining the state of actin-tropomyosin that is a central feature of the steric blocking mechanism of actin filament regulation.

show abstract

Localization and Mode of Action of the Inhibitory Protein Component of the Troponin Complex

Cited by 99 publications

References 0 publications

Effect of the troponin C‐like protein from bovine brain (brain modulator protein) on the Mg²⁺‐stimulated ATPase of skeletal muscle actomyosin

Effect of the troponin C‐like protein from bovine brain (brain modulator protein) on the Mg²⁺‐stimulated ATPase of skeletal muscle actomyosin

A ¹H NMR study of a ternary peptide complex that mimics the interaction between troponin C and troponin I

Tropomyosin and Troponin Regulation of Wild Type and E93K Mutant Actin Filaments from Drosophila Flight Muscle

Contact Info

Product

Resources

About

Localization and Mode of Action of the Inhibitory Protein Component of the Troponin Complex

Cited by 99 publications

References 0 publications

Effect of the troponin C‐like protein from bovine brain (brain modulator protein) on the Mg2+‐stimulated ATPase of skeletal muscle actomyosin

Effect of the troponin C‐like protein from bovine brain (brain modulator protein) on the Mg2+‐stimulated ATPase of skeletal muscle actomyosin

A 1H NMR study of a ternary peptide complex that mimics the interaction between troponin C and troponin I

Tropomyosin and Troponin Regulation of Wild Type and E93K Mutant Actin Filaments from Drosophila Flight Muscle

Contact Info

Product

Resources

About

Effect of the troponin C‐like protein from bovine brain (brain modulator protein) on the Mg²⁺‐stimulated ATPase of skeletal muscle actomyosin

Effect of the troponin C‐like protein from bovine brain (brain modulator protein) on the Mg²⁺‐stimulated ATPase of skeletal muscle actomyosin

A ¹H NMR study of a ternary peptide complex that mimics the interaction between troponin C and troponin I