Bisphosphorylation of cardiac troponin I modulates the Ca(2+)-dependent binding of myosin subfragment S1 to reconstituted thin filaments.

Abstract:

:We have reconstituted thin filaments comprising pyrene-labelled actin (pyr-actin), tropomyosin (Tm) and cardiac troponin (cTn). cTn was isolated in two defined phosphorylation states; completely dephosphorylated on all subunits and with only the cTnI subunit bisphosphorylated. The thin filament was saturated with cTn at a pyr-actin/Tm/cTn ratio of 7:1:1. The calcium-dependent binding of S1 to thin filaments was measured in a stopped-flow spectrophotometer and the dependence of the observed rate constant on [Ca2+] fitted to the Hill equation. The only significant difference between the two phosphorylation states of the filaments was a 0.36 decrease in the pCa50 on bisphosphorylation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Reiffert SU,Jaquet K,Heilmeyer LM Jr,Ritchie MD,Geeves MA

doi

10.1016/0014-5793(96)00274-8

subject

Has Abstract

pub_date

1996-04-08 00:00:00

pages

43-7

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)00274-8

journal_volume

384

pub_type

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