The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

ZIP1  -  Zip1p

Saccharomyces cerevisiae S288c

Synonyms: D9819.9, Synaptonemal complex protein ZIP1, YDR285W
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

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].

References

  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]
 
WikiGenes - Universities