Mutations in yeast calmodulin cause defects in spindle pole body functions and nuclear integrity

doi:10.1083/jcb.119.6.1625

This Article

Full Text (PDF, 7597K)

Alert me when this article is cited

Citation Map

Services

Email this article

Similar articles in this journal

Similar articles in PubMed

Alert me to new content in the JCB

Download to citation manager

Citing Articles

Citing Articles via HighWire

Citing Articles via CrossRef

Citing Articles via Google Scholar

Google Scholar

Articles by Sun, G. H.

Articles by Anraku, Y.

Search for Related Content

PubMed

PubMed Citation

Articles by Sun, G. H.

Articles by Anraku, Y.

Pubmed/NCBI databases

Gene	GEO Profiles
HomoloGene
Substance via MeSH

Social Bookmarking

What's this?

ARTICLES

Mutations in yeast calmodulin cause defects in spindle pole body functions and nuclear integrity

GH Sun, A Hirata, Y Ohya and Y Anraku
Department of Biology, Faculty of Science, University of Tokyo, Japan.

Yeast calmodulin (CaM) is required for the progression of nuclear division (Ohya, Y. and Y. Anraku. 1989. Curr. Genet. 15:113-120), although the precise mechanism and physiological role of CaM in this process are unclear. In this paper we have characterized the phenotype caused by a temperature-sensitive lethal mutation (cmdl-101) in the yeast CaM. The cmdl-101 mutation expresses a carboxyl-terminal half of the yeast CaM (Met72-Cys147) under the control of an inducible GAL1 promoter. Incubation of the cmdl-101 cells at a nonpermissive temperature causes a severe defect in chromosome segregation. The rate of chromosome loss in the cmdl-101 mutant is higher than wild-type cell even at permissive temperature. The primary visible defect observed by immunofluorescence and electron microscopic analyses is that the organization of spindle microtubules is abnormal in the cmdl-101 cells grown at nonpermissive temperature. Majority of budded cells arrested at the high temperature contain only one spindle pole body (SPB), which forms monopolar spindle, whereas the budded cells of the same strain incubated at permissive temperature all contain two SPBs. Using the freeze-substituted fixation method, we found that the integrity of the nuclear morphology of the cmdl-101 mutant cell is significantly disturbed. The nucleus in wild-type cells is round with smooth contours of nuclear envelope. However, the nuclear envelope in the mutant cells appears to be very flexible and forms irregular projections and invaginations that are never seen in wild-type cells. The deformation of the nuclear becomes much more severe as the incubation at nonpermissive temperature continues. The single SPB frequently localizes on the projections or the invaginations of the nuclear envelope. These observations suggest that CaM is required for the functions of SPB and spindle, and the integrity of nucleus.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Nishikawa, S.-i., Hirata, A., Endo, T. (2008). Nuclear inner membrane fusion facilitated by yeast Jem1p is required for spindle pole body fusion but not for the first mitotic nuclear division during yeast mating.. GENES CELLS 13: 1185-1195 [Abstract] [Full Text]
Kimata, Y., Ishiwata-Kimata, Y., Ito, T., Hirata, A., Suzuki, T., Oikawa, D., Takeuchi, M., Kohno, K. (2007). Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. JCB 179: 75-86 [Abstract] [Full Text]
Okano, H., Asakawa, M., Ohya, Y. (2004). A Novel Mechanism of Intragenic Complementation between Phe to Ala Calmodulin Mutations. J Biochem 135: 289-295 [Abstract] [Full Text]
Popescu, A., Miron, S., Blouquit, Y., Duchambon, P., Christova, P., Craescu, C. T. (2003). Xeroderma Pigmentosum Group C Protein Possesses a High Affinity Binding Site to Human Centrin 2 and Calmodulin. J. Biol. Chem. 278: 40252-40261 [Abstract] [Full Text]
Abe, M., Qadota, H., Hirata, A., Ohya, Y. (2003). Lack of GTP-bound Rho1p in secretory vesicles of Saccharomyces cerevisiae. JCB 162: 85-97 [Abstract] [Full Text]
Okuzaki, D., Satake, W., Hirata, A., Nojima, H. (2003). Fission yeast meu14+ is required for proper nuclear division and accurate forespore membrane formation during meiosis II. J. Cell Sci. 116: 2721-2735 [Abstract] [Full Text]
Misu, K., Fujimura-Kamada, K., Ueda, T., Nakano, A., Katoh, H., Tanaka, K. (2003). Cdc50p, a Conserved Endosomal Membrane Protein, Controls Polarized Growth in Saccharomyces cerevisiae. Mol. Biol. Cell 14: 730-747 [Abstract] [Full Text]
Tange, Y., Hirata, A., Niwa, O. (2002). An evolutionarily conserved fission yeast protein, Ned1, implicated in normal nuclear morphology and chromosome stability, interacts with Dis3, Pim1/RCC1 and an essential nucleoporin. J. Cell Sci. 115: 4375-4385 [Abstract] [Full Text]
Yahara, N., Ueda, T., Sato, K., Nakano, A. (2001). Multiple Roles of Arf1 GTPase in the Yeast Exocytic and Endocytic Pathways. Mol. Biol. Cell 12: 221-238 [Abstract] [Full Text]
Middendorp, S., Kuntziger, T., Abraham, Y., Holmes, S., Bordes, N., Paintrand, M., Paoletti, A., Bornens, M. (2000). A Role for Centrin 3 in Centrosome Reproduction. JCB 148: 405-416 [Abstract] [Full Text]
Yabe, I., Horiuchi, K.-i., Nakahara, K., Hiyama, T., Yamanaka, T., Wang, P.-C., Toda, K., Hirata, A., Ohsumi, Y., Hirata, R., Anraku, Y., Kusaka, I. (1999). Patch Clamp Studies on V-type ATPase of Vacuolar Membrane of Haploid Saccharomyces cerevisiae. PREPARATION AND UTILIZATION OF A GIANT CELL CONTAINING A GIANT VACUOLE. J. Biol. Chem. 274: 34903-34910 [Abstract] [Full Text]
Jurado, L. A., Chockalingam, P. S., Jarrett, H. W. (1999). Apocalmodulin. Physiol. Rev. 79: 661-682 [Abstract] [Full Text]
Adams, I. R., Kilmartin, J. V. (1999). Localization of Core Spindle Pole Body (SPB) Components during SPB Duplication in Saccharomyces cerevisiae. JCB 145: 809-823 [Abstract] [Full Text]
Sato, M., Sato, K., Nishikawa, S.-i., Hirata, A., Kato, J.-i., Nakano, A. (1999). The Yeast RER2 Gene, Identified by Endoplasmic Reticulum Protein Localization Mutations, Encodes cis-Prenyltransferase, a Key Enzyme in Dolichol Synthesis. Mol. Cell. Biol. 19: 471-483 [Abstract] [Full Text]
Moser, M., Flory, M., Davis, T. (1997). Calmodulin localizes to the spindle pole body of Schizosaccharomyces pombe and performs an essential function in chromosome segregation. J. Cell Sci. 110: 1805-1812 [Abstract]
Zarzov, P, Boucherie, H, Mann, C (1997). A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication. J. Cell Sci. 110: 1879-1891 [Abstract]
Wada, Y, Nakamura, N, Ohsumi, Y, Hirata, A (1997). Vam3p, a new member of syntaxin related protein, is required for vacuolar assembly in the yeast Saccharomyces cerevisiae. J. Cell Sci. 110: 1299-1306 [Abstract]
Stirling, D., Rayner, T., Prescott, A., Stark, M. (1996). Mutations which block the binding of calmodulin to Spc110p cause multiple mitotic defects. J. Cell Sci. 109: 1297-1310 [Abstract]
Moser, M. J., Lee, S. Y., Klevit, R. E., Davis, T. N. (1995). Ca[IMAGE] Binding to Calmodulin and Its Role in Schizosaccharomyces pombe as Revealed by Mutagenesis and NMR Spectroscopy. J. Biol. Chem. 270: 20643-20652 [Abstract] [Full Text]
Ohya, Y, Botstein, D (1994). Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263: 963-966 [Abstract]
Harris, E, Watterson, D., Thorner, J (1994). Functional consequences in yeast of single-residue alterations in a consensus calmodulin. J. Cell Sci. 107: 3235-3249 [Abstract]
Higashio, H., Kimata, Y., Kiriyama, T., Hirata, A., Kohno, K. (2000). Sfb2p, a Yeast Protein Related to Sec24p, Can Function as a Constituent of COPII Coats Required for Vesicle Budding from the Endoplasmic Reticulum. J. Biol. Chem. 275: 17900-17908 [Abstract] [Full Text]
Umebayashi, K., Fukuda, R., Hirata, A., Horiuchi, H., Nakano, A., Ohta, A., Takagi, M. (2001). Activation of the Ras-cAMP Signal Transduction Pathway Inhibits the Proteasome-independent Degradation of Misfolded Protein Aggregates in the Endoplasmic Reticulum Lumen. J. Biol. Chem. 276: 41444-41454 [Abstract] [Full Text]