Tropomyosin‐troponin complex stabilizes the pointed ends of actin filaments against polymerization and depolymerization
- 29 January 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 260 (2) , 266-268
- https://doi.org/10.1016/0014-5793(90)80119-4
Abstract
In striated muscle the pointed ends of polar actin filaments are directed toward the center of the sarcomer. Formed filaments keep a constant length of about 1 μm. As polymerization and depolymerization at free pointed ends are not sufficiently slow to account for the constant length of the filaments, we searched for proteins which occur in sarcomers and can stabilize the pointed ends of actin filaments. We observed that tropornyosintroponin complex reduces the rate of association and dissociation of actin molecules at the pointed ends more than 30-fold. On the average, every 600 s one association or dissociation reaction has been found to occur at the pointed ends near the critical actin monomer concentration.Keywords
This publication has 17 references indexed in Scilit:
- Tropomyosin inhibits the rate of actin polymerization by stabilizing actin filamentsBiochemistry, 1988
- Rate of binding of tropomyosin to actin filamentsBiochemistry, 1988
- Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments.The Journal of cell biology, 1986
- Rate of treadmilling of actin filaments in vitroJournal of Molecular Biology, 1986
- Isolation from bovine brain of tropomyosins that bind to actin filaments with different affinitiesFEBS Letters, 1985
- A Ca2+‐dependent actin modulator from vertebrate smooth muscleFEBS Letters, 1984
- Acumentin, a protein in macrophages which caps the ‘pointed’ end of actin filamentsNature, 1982
- Equilibrium of the actin-tropomyosin interactionJournal of Molecular Biology, 1979
- Head to tail polymerization of actinJournal of Molecular Biology, 1976
- Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscleJournal of Molecular Biology, 1963