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Gene Review

ZIP1  -  Zip1p

Saccharomyces cerevisiae S288c

Synonyms: D9819.9, Synaptonemal complex protein ZIP1, YDR285W
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High impact information on ZIP1


Biological context of ZIP1


Associations of ZIP1 with chemical compounds

  • Zip1 is predicted to form an alpha-helical coiled coil, flanked by globular domains at the NH(2) and COOH termini [9].
  • We discuss this regulation in S. cerevisiae and compare it with the regulation of two other transcriptional activators involved in cadmium detoxification: the Schizosaccharomyces pombe Zip1, regulated by SCF(Pof1), and the mammalian Nrf2, regulated by the SCF-like ubiquitin ligase Cul3:Rbx1:Keap1 [10].

Physical interactions of ZIP1


Regulatory relationships of ZIP1

  • Comparison of the expression of meiosis-specific Ndj1p-HA and Zip1p in haploid control and kar3Delta time courses revealed that fewer cells enter the meiotic cycle in absence of Kar3p [12].

Other interactions of ZIP1

  • In yeast, mutations of this type include rad50S, dmc1, rad51, and zip1 [4].
  • Crossing-over is decreased in the zip4 mutant (as in zip1, zip2, and zip3); the remaining crossovers are largely dependent on a parallel pathway utilizing Mms4. zip4 displays a novel phenotype: negative crossover interference, meaning that crossovers tend to cluster [13].
  • Overproduction of either the meiotic chromosomal protein Red1 or the meiotic kinase Mek1 bypasses this checkpoint, allowing zip1 cells to sporulate [14].
  • Physical analysis of meiotic recombination in a zip1 mutant reveals the following: Crossovers appear later than normal and at a reduced level [11].
  • In the absence of DOT1, the zip1 and dmc1 mutants inappropriately progress through meiosis, generating inviable meiotic products [15].

Analytical, diagnostic and therapeutic context of ZIP1

  • Our epitope mapping data indicate that the organization of Zip1 within polycomplexes is similar to that of the SC, whereas the organization of Zip1 within networks is fundamentally different [9].


  1. RecA homologs Dmc1 and Rad51 interact to form multiple nuclear complexes prior to meiotic chromosome synapsis. Bishop, D.K. Cell (1994) [Pubmed]
  2. Crossover interference is abolished in the absence of a synaptonemal complex protein. Sym, M., Roeder, G.S. Cell (1994) [Pubmed]
  3. ZIP1 is a synaptonemal complex protein required for meiotic chromosome synapsis. Sym, M., Engebrecht, J.A., Roeder, G.S. Cell (1993) [Pubmed]
  4. Meiotic cells monitor the status of the interhomolog recombination complex. Xu, L., Weiner, B.M., Kleckner, N. Genes Dev. (1997) [Pubmed]
  5. The yeast Red1 protein localizes to the cores of meiotic chromosomes. Smith, A.V., Roeder, G.S. J. Cell Biol. (1997) [Pubmed]
  6. The budding yeast Msh4 protein functions in chromosome synapsis and the regulation of crossover distribution. Novak, J.E., Ross-Macdonald, P.B., Roeder, G.S. Genetics (2001) [Pubmed]
  7. Two distinct surveillance mechanisms monitor meiotic chromosome metabolism in budding yeast. Wu, H.Y., Burgess, S.M. Curr. Biol. (2006) [Pubmed]
  8. Roles for two RecA homologs in promoting meiotic chromosome synapsis. Rockmill, B., Sym, M., Scherthan, H., Roeder, G.S. Genes Dev. (1995) [Pubmed]
  9. Organization of the yeast Zip1 protein within the central region of the synaptonemal complex. Dong, H., Roeder, G.S. J. Cell Biol. (2000) [Pubmed]
  10. Regulation of the cadmium stress response through SCF-like ubiquitin ligases: comparison between Saccharomyces cerevisiae, Schizosaccharomyces pombe and mammalian cells. Baudouin-Cornu, P., Labarre, J. Biochimie (2006) [Pubmed]
  11. Synaptonemal complex (SC) component Zip1 plays a role in meiotic recombination independent of SC polymerization along the chromosomes. Storlazzi, A., Xu, L., Schwacha, A., Kleckner, N. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  12. Increased ploidy and KAR3 and SIR3 disruption alter the dynamics of meiotic chromosomes and telomeres. Trelles-Sticken, E., Loidl, J., Scherthan, H. J. Cell. Sci. (2003) [Pubmed]
  13. The meiosis-specific zip4 protein regulates crossover distribution by promoting synaptonemal complex formation together with zip2. Tsubouchi, T., Zhao, H., Roeder, G.S. Dev. Cell (2006) [Pubmed]
  14. Bypass of a meiotic checkpoint by overproduction of meiotic chromosomal proteins. Bailis, J.M., Smith, A.V., Roeder, G.S. Mol. Cell. Biol. (2000) [Pubmed]
  15. Role for the silencing protein Dot1 in meiotic checkpoint control. San-Segundo, P.A., Roeder, G.S. Mol. Biol. Cell (2000) [Pubmed]
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