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Eukaryotic chaperonin containing T-complex polypeptide 1 interacts with filamentous actin and reduces the initial rate of actin polymerization in vitro

Grantham, J., Ruddock, Lloyd W., Roobol, Anne, Carden, Martin J. (2002) Eukaryotic chaperonin containing T-complex polypeptide 1 interacts with filamentous actin and reduces the initial rate of actin polymerization in vitro. Cell Stress and Chaperones, 7 (3). pp. 235-242. ISSN 1355-8145. (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:22876)

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Abstract

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.

Item Type: Article
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Funders: Biotechnology and Biological Sciences Research Council (https://ror.org/00cwqg982)
Depositing User: Martin Carden
Date Deposited: 02 Oct 2009 17:35 UTC
Last Modified: 12 Jul 2022 10:40 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/22876 (The current URI for this page, for reference purposes)
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