Grantham, J. and Ruddock, L.W. and Roobol, A. and Carden, M.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 .
|
PDF (Eukaryotic Chaperonin)
Restricted to Repository staff only |
|
|
| Contact us about this Publication
Download (583Kb)
|
![[img]](http://kar.kent.ac.uk/style/images/fileicons/application_pdf.png) |
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: | Faculties > Science Technology and Medical Studies > School of Biosciences |
| Depositing User: | Martin Carden |
| Date Deposited: | 02 Oct 2009 17:35 |
| Last Modified: | 06 Sep 2011 04:27 |
| Resource URI: | http://kar.kent.ac.uk/id/eprint/22876 (The current URI for this page, for reference purposes) |
- Depositors only (login required):
