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SLK19  -  Slk19p

Saccharomyces cerevisiae S288c

Synonyms: Kinetochore protein SLK19, Synthetic lethal KAR3 protein 19, YOR195W
 
 
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High impact information on SLK19

  • Here we show that separase also cleaves the kinetochore-associated protein Slk19 at anaphase onset [1].
  • The cleavage and localization of Slk19 are necessary to stabilize the anaphase spindle, and we show that a stable spindle is a prerequisite for timely exit from mitosis [1].
  • Strains with a deletion of SLK19 (synthetic lethal Kar3p gene) exhibit abnormally short mitotic spindles, increased numbers of astral microtubules, and require the presence of the kinesin motor Kar3p for viability [2].
  • A functional fusion of Slk19p to green fluorescent protein (GFP) localizes to kinetochores and, during anaphase, to the spindle midzone, whereas Kar3p-GFP was found at the nuclear side of the spindle pole body [2].
  • Slk19p is a centromere protein that functions to stabilize mitotic spindles [2].
 

Biological context of SLK19

  • We also demonstrate genetic interactions between DAM1 and CTF19 or SLK19 genes encoding kinetochore proteins [3].
  • Cells lacking the protein phosphatase CDC14 or its regulators, SPO12 and SLK19, undergo only a single meiotic division, with some chromosomes segregating reductionally and others equationally [4].
  • RESULTS: We show that the SLK19 gene product from Saccharomyces cerevisiae is essential for proper chromosome segregation during meiosis I [5].
  • Deletion analysis of these genes demonstrated that TPO1 and SLK19 specifically regulated ERG9 expression when tested with several different promoter-reporter gene fusions [6].
  • The MEN pathway was dispensable for condensin-to-rDNA targeting, however MEN-mediated release of Cdc14p later in anaphase allowed for proper, albeit delayed, condensin targeting to rDNA and successful segregation of nucleolus in the slk19 FEAR mutant [7].
 

Anatomical context of SLK19

  • The fraction of slk19 delta cells that were able to form tetrads solely exhibited YAC segregation defects in meiosis II, whereas the segregation of YACs in meiosis I was normal in these cells [8].
 

Enzymatic interactions of SLK19

 

Regulatory relationships of SLK19

  • Additionally, EMSAs demonstrated that extracts derived from the TPO1 deletion strain was unable to shift the repressing cis-element while protein extracts from the SLK19 deletion strain had a reduced shift of the activating cis-element [6].
 

Other interactions of SLK19

References

  1. Orchestrating anaphase and mitotic exit: separase cleavage and localization of Slk19. Sullivan, M., Lehane, C., Uhlmann, F. Nat. Cell Biol. (2001) [Pubmed]
  2. Slk19p is a centromere protein that functions to stabilize mitotic spindles. Zeng, X., Kahana, J.A., Silver, P.A., Morphew, M.K., McIntosh, J.R., Fitch, I.T., Carbon, J., Saunders, W.S. J. Cell Biol. (1999) [Pubmed]
  3. Yeast Dam1p has a role at the kinetochore in assembly of the mitotic spindle. Jones, M.H., He, X., Giddings, T.H., Winey, M. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  4. The Cdc14 phosphatase and the FEAR network control meiotic spindle disassembly and chromosome segregation. Marston, A.L., Lee, B.H., Amon, A. Dev. Cell (2003) [Pubmed]
  5. Slk19p is necessary to prevent separation of sister chromatids in meiosis I. Kamieniecki, R.J., Shanks, R.M., Dawson, D.S. Curr. Biol. (2000) [Pubmed]
  6. Positive and negative regulation of squalene synthase (ERG9), an ergosterol biosynthetic gene, in Saccharomyces cerevisiae. Kennedy, M.A., Bard, M. Biochim. Biophys. Acta (2001) [Pubmed]
  7. Cdc14p/FEAR pathway controls segregation of nucleolus in S. cerevisiae by facilitating condensin targeting to rDNA chromatin in anaphase. Wang, B.D., Yong-Gonzalez, V., Strunnikov, A.V. Cell Cycle (2004) [Pubmed]
  8. The yeast kinetochore protein Slk19 is required to prevent aberrant chromosome segregation in meiosis and mitosis. Pfiz, S., Zimmermann, J., Hilt, W. Genes Cells (2002) [Pubmed]
  9. Studies on substrate recognition by the budding yeast separase. Sullivan, M., Hornig, N.C., Porstmann, T., Uhlmann, F. J. Biol. Chem. (2004) [Pubmed]
 
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