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© The Rockefeller University Press, 0021-9525/1997//1271 $5.00
The Journal of Cell Biology, Volume 139, Number 5, , 1997 1271-1280

Article

Stu2p: A Microtubule-Binding Protein that Is an Essential Component of the Yeast Spindle Pole Body



Peijing Jeremy Wang and Tim C. Huffaker

Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853

Previously we isolated tub2-423, a cold-sensitive allele of the Saccharomyces cerevisiae gene encoding β-tubulin that confers a defect in mitotic spindle function. In an attempt to identify additional proteins that are important for spindle function, we screened for suppressors of the cold sensitivity of tub2-423 and obtained two alleles of a novel gene, STU2. STU2 is an essential gene and encodes a protein whose sequence is similar to proteins identified in a variety of organisms. Stu2p localizes primarily to the spindle pole body (SPB) and to a lesser extent along spindle microtubules. Localization to the SPB is not dependent on the presence of microtubules, indicating that Stu2p is an integral component of the SPB. Stu2p also binds microtubules in vitro. We have localized the microtubule-binding domain of Stu2p to a highly basic 100-amino acid region. This region contains two imperfect repeats; both repeats appear to contribute to microtubule binding to similar extents. These results suggest that Stu2p may play a role in the attachment, organization, and/or dynamics of microtubule ends at the SPB.

Abbreviations used in this paper: DAPI, 4',6-diamidino-2-phenylindole; GFP, green fluorescent protein; HA, hemagglutinin, MTOC, microtubule-organizing center; ORF, open reading frame; SPB, spindle pole body.

Address all correspondence to Tim Huffaker, Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853. Tel.: (607) 255-9947. Fax: (607) 255-2428. E-mail:tch4{at}cornell.edu


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