Premium
Essential role of tubulin‐folding cofactor D in microtubule assembly and its association with microtubules in fission yeast
Author(s) -
Hirata Dai,
Masuda Hirohisa,
Eddison Mark,
Toda Takashi
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.3.658
Subject(s) - biology , microtubule , tubulin , fission , yeast , folding (dsp implementation) , microtubule associated protein , microbiology and biotechnology , schizosaccharomyces , cofactor , biophysics , saccharomyces cerevisiae , biochemistry , schizosaccharomyces pombe , enzyme , nuclear physics , physics , neutron , engineering , electrical engineering
The main structural components of microtubules are α‐ and β‐tubulins. A group of proteins called cofactors are crucial in the formation of assembly‐competent tubulin molecules in vitro . Whilst an in vitro role is emerging for these cofactors, their biological functions in vivo remain to be established. In order to understand the fundamental mechanisms that determine cell polarity, we have screened for fission yeast mutants with altered polarity. Here we show that alp1 + encodes a homologue of cofactor D and executes a function essential for cell viability. A temperature‐sensitive alp1 mutant shows a variety of defects including abnormal mitoses, loss of microtubule structures, displacement of the nucleus, altered growth polarity and asymmetrical cell division. Overexpression of Alp1 is lethal in wild‐type cells, resulting in altered cell shape, but is rescued by co‐overexpression of β‐tubulin. Alp1 co‐localizes with microtubules, both interphase arrays and mitotic spindles. Furthermore, Alp1 binds to and co‐sediments with taxol (paclitaxel)‐stabilized porcine microtubules. Our results suggest that, in addition to a function in the folding of β‐tubulin, cofactor D may play a vital role in microtubule‐dependent processes as a microtubule‐associated protein.