We have previously observed that subunits of the chaperonin required for actin production (type-II chaperonin containing T-complex polypeptide 1 [CCT]) localize at sites of microfilament assembly. In this article we extend this observation by showing that substantially substoichiometric CCT reduces the initial rate of pyrene-labeled actin polymerization in vitro where eubacterial chaperonin GroEL had no such effect. CCT subunits bound selectively to F-actin in cosedimentation assays, and CCT reduced elongation rates from both purified actin filament “seeds” and the short and stabilized, minus-end blocked filaments in erythrocyte membrane cytoskeletons. These observations suggest CCT might remain involved in biogenesis of the actin cytoskeleton, by acting at filament ( ) ends, beyond its already well-established role in producing new actin monomers.
How to translate text using browser tools
1 July 2002
Eukaryotic chaperonin containing T-complex polypeptide 1 interacts with filamentous actin and reduces the initial rate of actin polymerization in vitro
Julie Grantham,
Lloyd W. Ruddock,
Anne Roobol,
Martin J. Carden
ACCESS THE FULL ARTICLE
It is not available for individual sale.
This article is only available to subscribers.
It is not available for individual sale.
It is not available for individual sale.