The spindle pole body component Spc98p interacts with the γ‐tubulin-like Tub4p of Saccharomyces cerevisiae at the sites of microtubule attachment

• Verfasst von: Geißler, Silke [VerfasserIn]
• Verfasst von: Pereira, Gislene [VerfasserIn]
• Verfasst von: Knop, Michael [VerfasserIn]
• Verfasst von: Schiebel, Elmar [VerfasserIn]
• Titel: The spindle pole body component Spc98p interacts with the γ‐tubulin-like Tub4p of Saccharomyces cerevisiae at the sites of microtubule attachment
• Verf.angabe: Silke Geissler, Gislene Pereira, Anne Spang, Michael Knop, Sylvie Souès, John Kilmartin and Elmar Schiebel
• Umfang: 13 S.
• Fussnoten: Gesehen am 31.08.2017
• Titel Quelle: Enthalten in: European Molecular Biology Organization: The EMBO journal
• Jahr Quelle: 1996
• Band/Heft Quelle: 15(1996), 15, S. 3899-3911
• ISSN Quelle: 1460-2075
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1562960083

Abstract

Tub4p is a novel tubulin found in Saccharomyces cerevisiae. It most resembles gamma-tubulin and, like it, is localized to the yeast microtubule organizing centre, the spindle pole body (SPB). In this paper we report the identification of SPC98 as a dosage-dependent suppressor of the conditional lethal tub4-1 allele. SPC98 encodes an SPB component of 98 kDa which is identical to the previously described 90 kDa SPB protein. Strong overexpression of SPC98 is toxic, causing cells to arrest with a large bud, defective microtubule structures, undivided nucleus and replicated DNA. The toxicity of SPC98 overexpression was relieved by co-overexpression of TUB4. Further evidence for an interaction between Tub4p and Spc98p came from the synthetic toxicity of tub4-1 and spc98-1 alleles, the dosage-dependent suppression of spc98-4 by TUB4, the binding of Tub4p to Spc98p in the two-hybrid system and the co-immunoprecipitation of Tub4p and Spc98p. In addition, Spc98-1p is defective in its interaction with Tub4p in the two-hybrid system. We suggest a model in which Tub4p and Spc98p form a complex involved in microtubule organization by the SPB.