Yeast, tubulin cofactors

Tubulins are among the most highly conserved proteins known, and it is therefore not surprising that homologs of the cofactors that participate in the biogenesis of heterodimers in mammals should exist in yeast cells (Table I). On the other hand, it is somewhat surprising that, while... 

In contrast to S. cerevisiae, the microtubule cytoskeleton in the fission yeast Schizosacaromyces pombe is more complex and the amino acid sequences of the tubulin polypeptides are closer to mammalian sequences. The fission yeast homologs of cofactors B, D, and E are essential for survival in this organism. It seems highly likely that the cofactors are also essential for life in ciliates, flagellates, and multicellular organisms, in which the sequence of tubulins are also highly conserved. 

Archer, J. E., L. R. Vega, and F. Solomon (1995). Rbl2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo. Cell 82, 425-434. Bhamidipati, A., S. A. Lewis, and N. J. Cowan (2000). ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin. J. Cell. Biol. 149, 1087-1096. 

Grishchuk, E. L., and J. R. McIntosh (1999). Sto lp, a fission yeast protein similar to tubulin folding cofactor E, plays an essential role in mitotic microtubule assembly. J. CeUSci. 112, 1979-1988. 

Hirata, D., H. Masuda, M. Eddison, and T. Toda (1998). Essential role of tubulin-folding cofactor D in microtubule assembly and its association with microtubules in fission yeast. EMBO J. 17, 658-666. 

Radcliffe, P. A., D. Hirata, L. Vardy, and T. Toda (1999). Functional dissection and hierarchy of tubulin-folding cofactors in fission yeasts. Mol. Biol Cell 10, 2987-3001. 

Radcliffe, P. A., and T. Toda (2000). Characterisation of fission yeast alp 11 mutants defines three functional domains within tubulin-folding cofactor B. Mol Gen. Genet. 263, 752-760. 

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