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1 July 2002 Eukaryotic chaperonin containing T-complex polypeptide 1 interacts with filamentous actin and reduces the initial rate of actin polymerization in vitro
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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.

Julie Grantham, Lloyd W. Ruddock, Anne Roobol, and Martin J. Carden "Eukaryotic chaperonin containing T-complex polypeptide 1 interacts with filamentous actin and reduces the initial rate of actin polymerization in vitro," Cell Stress & Chaperones 7(3), 235-242, (1 July 2002). https://doi.org/10.1379/1466-1268(2002)007<0235:ECCTCP>2.0.CO;2
Received: 25 September 2001; Accepted: 1 January 2002; Published: 1 July 2002
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