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Molecular and Cellular Biology, January 2002, p. 138-147, Vol. 22, No. 1
0270-7306/01/$04.00+0     DOI: 10.1128/MCB.22.1.138-147.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Protection from Free ß-Tubulin by the ß-Tubulin Binding Protein Rbl2p

Katharine C. Abruzzi, Adelle Smith, William Chen, and Frank Solomon*

Department of Biology and Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Received 14 June 2001/ Returned for modification 2 August 2001/ Accepted 3 October 2001

Free ß-tubulin not in heterodimers with {alpha}-tubulin can be toxic, disrupting microtubule assembly and function. We are interested in the mechanisms by which cells protect themselves from free ß-tubulin. This study focused specifically on the function of Rbl2p, which, like {alpha}-tubulin, can rescue cells from free ß-tubulin. In vitro studies of the mammalian homolog of Rbl2p, cofactor A, have suggested that Rbl2p/cofactor A may be involved in tubulin folding. Here we show that Rbl2p becomes essential in cells containing a modest excess of ß-tubulin relative to {alpha}-tubulin. However, this essential activity of Rbl2p/cofactorA does not depend upon the reactions described by the in vitro assay. Rescue of ß-tubulin toxicity requires a minimal but substoichiometric ratio of Rbl2p to ß-tubulin. The data suggest that Rbl2p binds transiently to free ß-tubulin, which then passes into an aggregated form that is not toxic.

* Corresponding author. Mailing address: Building E17, Room 220, Massachusetts Institute of Technology, Cambridge, MA 02139. Phone: (617) 253 3026. Fax: (617) 253 6272. E-mail: solomon{at}mit.edu.

Molecular and Cellular Biology, January 2002, p. 138-147, Vol. 22, No. 1
0022-538X/01/$04.00+0     DOI: 10.1128/MCB.22.1.138-147.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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