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Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences of the United States of America 96(1999), 11, Seite 6205-6210 |
|---|---|
| Personen und Körperschaften: | , , |
| Titel: | Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication/ Sarah Elliott, Michael Knop, Gabriel Schlenstedt, and Elmar Schiebel |
| Format: | E-Book-Kapitel |
| Sprache: | Englisch |
| veröffentlicht: |
May 25, 1999
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| Gesamtaufnahme: |
National Academy of Sciences (Washington, DC): Proceedings of the National Academy of Sciences of the United States of America, 96(1999), 11, Seite 6205-6210
, volume:96 |
| Quelle: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
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| 245 | 1 | 0 | |a Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication |c Sarah Elliott, Michael Knop, Gabriel Schlenstedt, and Elmar Schiebel |
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| 520 | |a 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. | ||
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| author | Elliott, Sarah, Knop, Michael, Schiebel, Elmar |
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| contents | 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. |
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| spelling | Elliott, Sarah VerfasserIn (DE-588)1138860743 (DE-627)896525961 (DE-576)492753040 aut, Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication Sarah Elliott, Michael Knop, Gabriel Schlenstedt, and Elmar Schiebel, May 25, 1999, 6, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Gesehen am 25.08.2017, 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., Knop, Michael VerfasserIn (DE-588)1064187552 (DE-627)813076749 (DE-576)423832107 aut, Schiebel, Elmar 1960- VerfasserIn (DE-588)1034622595 (DE-627)746029462 (DE-576)165868597 aut, Enthalten in National Academy of Sciences (Washington, DC) Proceedings of the National Academy of Sciences of the United States of America Washington, DC : National Acad. of Sciences, 1915 96(1999), 11, Seite 6205-6210 Online-Ressource (DE-627)254235379 (DE-600)1461794-8 (DE-576)073260509 1091-6490 nnns, volume:96 year:1999 number:11 pages:6205-6210 extent:6, http://dx.doi.org/10.1073/pnas.96.11.6205 Verlag Resolving-System kostenfrei Volltext, http://www.pnas.org/content/96/11/6205 Verlag kostenfrei Volltext, http://dx.doi.org/10.1073/pnas.96.11.6205 LFER, LFER 2017-09-14T00:00:00Z |
| spellingShingle | Elliott, Sarah, Knop, Michael, Schiebel, Elmar, Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication, 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. |
| swb_id_str | 492753059 |
| title | Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication |
| title_auth | Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication |
| title_full | Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication Sarah Elliott, Michael Knop, Gabriel Schlenstedt, and Elmar Schiebel |
| title_fullStr | Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication Sarah Elliott, Michael Knop, Gabriel Schlenstedt, and Elmar Schiebel |
| title_full_unstemmed | Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication Sarah Elliott, Michael Knop, Gabriel Schlenstedt, and Elmar Schiebel |
| title_in_hierarchy | Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication / Sarah Elliott, Michael Knop, Gabriel Schlenstedt, and Elmar Schiebel, |
| title_short | Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication |
| title_sort | spc29p is a component of the spc110p subcomplex and is essential for spindle pole body duplication |
| url | http://dx.doi.org/10.1073/pnas.96.11.6205, http://www.pnas.org/content/96/11/6205 |