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The Delta 14 mutation of human cardiac troponin T enhances ATPase activity and alters the cooperative binding of S1-ADP to regulated actin.

Abstract：

:The complex of tropomyosin and troponin binds to actin and inhibits activation of myosin ATPase activity and force production of striated muscles at low free Ca(2+) concentrations. Ca(2+) stimulates ATP activity, and at subsaturating actin concentrations, the binding of NEM-modified S1 to actin-tropomyosin-troponin increases the rate of ATP hydrolysis even further. We show here that the Delta14 mutation of troponin T, associated with familial hypertrophic cardiomyopathy, results in an increase in ATPase rate like that seen with wild-type troponin in the presence of NEM-S1. The enhanced ATPase activity was not due to a decreased incorporation of mutant troponin T with troponin I and troponin C to form an active troponin complex. The activating effect was more prominent with a hybrid troponin (skeletal TnI, TnC, and cardiac TnT) than with all cardiac troponin. Thus it appears that changes in the troponin-troponin contacts that result from mutations or from forming hybrids stabilize a more active state of regulated actin. An analysis of the effect of the Delta14 mutation on the equilibrium binding of S1-ADP to actin was consistent with stabilization of an active state of actin. This change in activation may be important in the development of cardiac disease.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Gafurov B,Fredricksen S,Cai A,Brenner B,Chase PB,Chalovich JM

doi

10.1021/bi048646h

subject

Has Abstract

pub_date

2004-12-07 00:00:00

pages

15276-85

issue

48

eissn

0006-2960

issn

1520-4995

journal_volume

43

pub_type

杂志文章

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