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Verfasst von:Elliott, Sarah [VerfasserIn]   i
 Knop, Michael [VerfasserIn]   i
 Schiebel, Elmar [VerfasserIn]   i
Titel:Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication
Verf.angabe:Sarah Elliott, Michael Knop, Gabriel Schlenstedt, and Elmar Schiebel
Umfang:6 S.
Fussnoten:Gesehen am 25.08.2017
Titel Quelle:Enthalten in: National Academy of Sciences (Washington, DC): Proceedings of the National Academy of Sciences of the United States of America
Jahr Quelle:1999
Band/Heft Quelle:96(1999), 11, S. 6205-6210
ISSN Quelle:1091-6490
Abstract:In yeast, microtubules are organized by the spindle pole body (SPB). The SPB is a disk-like multilayered structure that is embedded in the nuclear envelope via its central plaque, whereas the outer and inner plaques are exposed to the cytoplasm and nucleoplasm, respectively. How the SPB assembles is poorly understood. We show that the inner/central plaque is composed of a stable SPB subcomplex, containing the γ-tubulin complex-binding protein Spc110p, calmodulin, Spc42p, and Spc29p. Spc29p acts as a linker between the central plaque component Spc42p and the inner plaque protein Spc110p. Evidence is provided that the calmodulin-binding site of Spc110p influences the binding of Spc29p to Spc110p. Spc42p also was identified as a component of a cytoplasmic SPB subcomplex containing Spc94p/Nud1p, Cnm67p, and Spc42p. Spc29p and Spc42p may be part of a critical interface of nucleoplasmic and cytoplasmic assembled SPB subcomplexes that form during SPB duplication. In agreement with this, overexpressed Spc29p was found to be a nuclear protein, whereas Spc42p is cytoplasmic. In addition, an essential function of SPC29 during SPB assembly is indicated by the SPB duplication defect of conditional lethal spc29(ts) cells and by the genetic interaction of SPC29 with CDC31 and KAR1, two genes that are involved in SPB duplication.
DOI:doi:10.1073/pnas.96.11.6205
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Kostenfrei: Verlag: http://dx.doi.org/10.1073/pnas.96.11.6205
 Kostenfrei: Verlag: http://www.pnas.org/content/96/11/6205
 DOI: https://doi.org/10.1073/pnas.96.11.6205
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1562753053
Verknüpfungen:→ Zeitschrift

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