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Gene Review

MCM10  -  Mcm10p

Saccharomyces cerevisiae S288c

Synonyms: DNA43, Minichromosome maintenance protein 10, Protein DNA43, YIL150C
 
 
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High impact information on MCM10

 

Biological context of MCM10

 

Anatomical context of MCM10

  • Mcm10p is an abundant protein (approximately 4 x 10(4) copies per haploid cell) that is almost exclusively localized in the chromatin and/or nuclear matrix fractions during all phases of the cell cycle [6].
 

Physical interactions of MCM10

  • Mcm10p functionally interacts with components of the pre-replicative complex (Mcm2-Mcm7 complex and origin recognition complex) as well as the pre-initiation complex component (Cdc45p) suggesting that it may be a component of the pre-RC as well as the pre-IC [3].
  • Moreover, overexpressed Cdc17 that is normally subject to rapid degradation is stabilized by Mcm10 co-overexpression but not by co-overexpression of the B-subunit of pol-alpha, Pol12 [7].
  • A motif search revealed a match to the proliferating cell nuclear antigen (PCNA)-interacting protein (PIP) box in Mcm10 [8].
 

Regulatory relationships of MCM10

  • Furthermore, mutations in MCM10 inhibit the ability of GBD-SIR3 to restore silencing when tethered to a defective HMR-E [5].
  • Fission yeast Cdc23/Mcm10 functions after pre-replicative complex formation to promote Cdc45 chromatin binding [9].
 

Other interactions of MCM10

  • Consistent with a direct silencing function, Mcm10p shows a two-hybrid interaction with Sir2p and Sir3p that is destroyed by the mcm10-1 mutation and dependent on the C-terminal 108 amino acids [5].
  • We screened for mutations that are lethal in combination with mcm10-1 and obtained seven mutants named slm1-slm6 for synthetically lethal with mcm10 [3].
  • DNA sequence analysis suggested that DNA43 and DNA52 encode proteins of 59.6 and 80.6 kDa, respectively [10].
  • The high degree of evolutionary conservation of this domain implies that stabilizing Cdc17 may be a conserved function of Mcm10 [7].
  • A conserved Hsp10-like domain in Mcm10 is required to stabilize the catalytic subunit of DNA polymerase-alpha in budding yeast [7].
 

Analytical, diagnostic and therapeutic context of MCM10

References

  1. Mcm10 and the MCM2-7 complex interact to initiate DNA synthesis and to release replication factors from origins. Homesley, L., Lei, M., Kawasaki, Y., Sawyer, S., Christensen, T., Tye, B.K. Genes Dev. (2000) [Pubmed]
  2. Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha. Ricke, R.M., Bielinsky, A.K. Mol. Cell (2004) [Pubmed]
  3. Budding yeast mcm10/dna43 mutant requires a novel repair pathway for viability. Araki, Y., Kawasaki, Y., Sasanuma, H., Tye, B.K., Sugino, A. Genes Cells (2003) [Pubmed]
  4. The Cdc23 (Mcm10) protein is required for the phosphorylation of minichromosome maintenance complex by the Dfp1-Hsk1 kinase. Lee, J.K., Seo, Y.S., Hurwitz, J. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  5. Mcm10 is required for the maintenance of transcriptional silencing in Saccharomyces cerevisiae. Liachko, I., Tye, B.K. Genetics (2005) [Pubmed]
  6. Interactions between Mcm10p and other replication factors are required for proper initiation and elongation of chromosomal DNA replication in Saccharomyces cerevisiae. Kawasaki, Y., Hiraga, S., Sugino, A. Genes Cells (2000) [Pubmed]
  7. A conserved Hsp10-like domain in Mcm10 is required to stabilize the catalytic subunit of DNA polymerase-alpha in budding yeast. Ricke, R.M., Bielinsky, A.K. J. Biol. Chem. (2006) [Pubmed]
  8. Interaction between PCNA and diubiquitinated Mcm10 is essential for cell growth in budding yeast. Das-Bradoo, S., Ricke, R.M., Bielinsky, A.K. Mol. Cell. Biol. (2006) [Pubmed]
  9. Fission yeast Cdc23/Mcm10 functions after pre-replicative complex formation to promote Cdc45 chromatin binding. Gregan, J., Lindner, K., Brimage, L., Franklin, R., Namdar, M., Hart, E.A., Aves, S.J., Kearsey, S.E. Mol. Biol. Cell (2003) [Pubmed]
  10. Genetic and molecular analysis of DNA43 and DNA52: two new cell-cycle genes in Saccharomyces cerevisiae. Solomon, N.A., Wright, M.B., Chang, S., Buckley, A.M., Dumas, L.B., Gaber, R.F. Yeast (1992) [Pubmed]
 
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