Formation and Function of the Rbl2p-beta-Tubulin Complex
Abstract
The yeast protein Rbl2p suppresses the deleterious effects of excess beta-tubulin as efficiently as does alpha-tubulin. Both in vivo and in vitro, Rbl2p forms a complex with beta-tubulin that does not contain alpha-tubulin, thus defining a second pool of beta-tubulin in the cell. Formation of the complex depends upon the conformation of beta-tubulin. Newly synthesized beta-tubulin can bind to Rbl2p before it binds to alpha-tubulin. Rbl2p can also bind beta-tubulin from the alpha/beta-tubulin heterodimer, apparently by competing with alpha-tubulin. The Rbl2p-beta-tubulin complex has a half-life of ~2.5 h and is less stable than the alpha/beta-tubulin heterodimer. The results of our experiments explain both how excess Rbl2p can rescue cells overexpressing beta-tubulin and how it can be deleterious in a wild-type background. They also suggest that the Rbl2p-beta-tubulin complex is part of a cellular mechanism for regulating the levels and dimerization of tubulin chains.
Additional Information
Copyright © 1998, American Society for Microbiology. Received 3 July 1997/Returned for modification 22 August 1997/Accepted 22 December 1997 We thank R. Williams (Vanderbilt University) and M. Caplow (University of North Carolina) for discussions of heterodimer dissociation and the members of our laboratory for critical contributions. J.E.A. was supported in part by an NSF predoctoral fellowship. L.R.V. was supported in part by a predoctoral fellowship from HHMI. This work was supported by a grant from the NIH to F.S.Files
| Name | Size | Download all |
|---|---|---|
|
md5:6548cfa27226a35cf0de61f30e5e02bf
|
295.2 kB | Preview Download |
Additional details
- Eprint ID
- 1726
- Resolver ID
- CaltechAUTHORS:ARCmcb98
- Created
-
2006-02-13Created from EPrint's datestamp field
- Updated
-
2019-10-02Created from EPrint's last_modified field