dc.contributor.author | Oakley, Berl R. | |
dc.contributor.author | Horio, Tetsuya | |
dc.date.accessioned | 2015-04-21T20:38:04Z | |
dc.date.available | 2015-04-21T20:38:04Z | |
dc.date.issued | 1994-09-15 | |
dc.identifier.citation | Horio, T., & Oakley, B. (1994). Human gamma-tubulin functions in fission yeast. The Journal of Cell Biology, 126(6), 1465-1473. http://www.dx.doi.org/10.1083/jcb.126.6.1465 | en_US |
dc.identifier.issn | 0021-9525 | |
dc.identifier.uri | http://hdl.handle.net/1808/17456 | |
dc.description | This is the publisher's version, also available electronically from "http://jcb.rupress.org". | en_US |
dc.description.abstract | gamma-Tubulin is a phylogenetically conserved component of microtubule-organizing centers that is essential for viability and microtubule function. To examine the functional conservation of gamma-tubulin, we have tested the ability of human gamma-tubulin to function in the fission yeast Schizosaccharomyces pombe. We have found that expression of a human gamma-tubulin cDNA restores viability and a near-normal growth rate to cells of S. pombe lacking endogenous gamma-tubulin. Immunofluorescence microscopy showed that these cells contained normal mitotic spindles and interphase microtubule arrays, and that human gamma-tubulin, like S. pombe gamma-tubulin, localized to spindle pole bodies, the fungal microtubule-organizing centers. These results demonstrate that human gamma-tubulin functions in fission yeast, and they suggest that in spite of the great morphological differences between the microtubule-organizing centers of humans and fission yeasts, gamma-tubulin is likely to perform the same tasks in both. They suggest, moreover, that the proteins that interact with gamma-tubulin, including, most obviously, microtubule-organizing center proteins, must also be conserved. We have also found that a fivefold overexpression of S. pombe gamma-tubulin causes no reduction in growth rates or alteration of microtubule organization. We hypothesize that the excess gamma-tubulin is maintained in the cytoplasm in a form incapable of nucleating microtubule assembly. Finally, we have found that expression of human gamma-tubulin or overexpression of S. pombe gamma-tubulin causes no significant alteration of resistance to the antimicrotubule agents benomyl, thiabendazole and nocodazole. | en_US |
dc.publisher | Rockefeller University Press | en_US |
dc.title | Human gamma-tubulin functions in fission yeast | en_US |
dc.type | Article | |
kusw.kuauthor | Oakley, Berl R. | |
kusw.kudepartment | Molecular Biosciences | en_US |
dc.identifier.doi | 10.1083/jcb.126.6.1465 | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item does not meet KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess | |