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Vol. 10, Issue 9, 2987-3001, September 1999
Laboratory of Cell Regulation, Imperial Cancer Research Fund,
London WC2A 3PX, United Kingdom
We describe the isolation of fission yeast homologues of
tubulin-folding cofactors B (Alp11) and E (Alp21), which are essential for cell viability and the maintenance of microtubules.
Alp11B contains the glycine-rich motif (the CLIP-170
domain) involved in microtubular functions, whereas, unlike mammalian
cofactor E, Alp21E does not. Both mammalian and yeast
cofactor E, however, do contain leucine-rich repeats.
Immunoprecipitation analysis shows that Alp11B interacts
with both 
-tubulin and Alp21E, but not with the cofactor
D homologue Alp1, whereas Alp21E also interacts with
Alp1D. The cellular amount of -tubulin is decreased in
both alp1 and alp11 mutants.
Overproduction of Alp11B results in cell lethality and the
disappearance of microtubules, which is rescued by
co-overproduction of -tubulin. Both full-length Alp11B
and the C-terminal third containing the CLIP-170 domain localize in the
cytoplasm, and this domain is required for efficient binding to
-tubulin. Deletion of alp11 is suppressed by
multicopy plasmids containing either alp21+
or alp1+, whereas alp21
deletion is rescued by overexpression of
alp1+ but not
alp11+. Finally, the alp1
mutant is not complemented by either alp11+
or alp21+. The results suggest that
cofactors operate in a linear pathway (Alp11B-Alp21E-Alp1D), each with
distinct roles.
Corresponding author. E-mail address:
toda{at}europa.lif.icnet.uk.
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