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A Novel Step in ß-Tubulin Folding Is Important for Heterodimer Formation in Saccharomyces cerevisiae
Soni Lacefielda and Frank Solomonaa Department of Biology and Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
Corresponding author: Frank Solomon, Room 220, M.I.T., Cambridge, MA 02139., solomon{at}mit.edu (E-mail)
Communicating editor: F. WINSTON
-tubulin are unbalanced or if the tubulin heterodimer dissociates. We are using the toxicity of ß-tubulin to understand early steps in microtubule morphogenesis. We find that deletion of PLP1 suppresses toxic ß-tubulin formed by disparate levels of - and ß-tubulin. That suppression occurs either when -tubulin is modestly underexpressed relative to ß-tubulin or when ß-tubulin is inducibly and strongly overexpressed. Plp1p does not affect tubulin expression. Instead, a significant proportion of the undimerized ß-tubulin in plp1
cells is less toxic than that in wild-type cells. It is also less able to combine with -tubulin to form a heterodimer. As a result, plp1 cells have lower levels of heterodimer. Importantly, plp1 cells that also lack Pac10, a component of the GimC/PFD complex, are even less affected by free ß-tubulin. Our results suggest that Plp1p defines a novel early step in ß-tubulin folding.
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