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RPN12  -  proteasome regulatory particle lid subunit...

Saccharomyces cerevisiae S288c

Synonyms: 26S proteasome regulatory subunit RPN12, NIN1, Nuclear integrity protein 1, YFR052W
 
 
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High impact information on RPN12

  • Cytokinin growth responses in Arabidopsis involve the 26S proteasome subunit RPN12 [1].
  • In yeast, RPN12 is necessary for the G1/S and G2/M transitions of the cell cycle, phases that have been shown to be under cytokinin control in plants [1].
  • In striking contrast, Sic1 turnover is severely impaired by a temperature-sensitive mutation in RPN12/NIN1, encoding another essential RP subunit [2].
  • The SEN3 also was identified in a synthetic lethal screen with the nin1-1 mutant, a temperature-sensitive mutant of NIN1 [3].
  • The deduced amino acid sequences of both mts3+ and NIN1 show homology to peptide sequences obtained from subunit 14 of the 26 S protease purified from bovine or human cells [4].
 

Biological context of RPN12

  • Genetic evidence for interaction between components of the yeast 26S proteasome: combination of a mutation in RPN12 (a lid component gene) with mutations in RPT1 (an ATPase gene) causes synthetic lethality [5].
  • We identified a new essential gene of Saccharomyces cerevisiae, designated NIN1 (nuclear integrity) [6].
  • In this study, a genetic event occurring in the nin1-1 mutant was found to be a frameshift mutation, resulting in a truncated protein smaller than the wild-type Nin1 protein [7].
  • Disruption of NIN1 resulted in cell death; however, a dead spore clone contained about 30 dead cells, indicating that spores that received the disrupted nin1 allele divided approximately five times before their death [6].
  • NIN1 is mapped on chromosome VI, 16 cM centromere-distal to PHO4 [6].
 

Physical interactions of RPN12

  • We propose that this region is necessary for Rpt1 to interact with Rpn12 [5].
 

Other interactions of RPN12

  • The resultant precipitate contained Nin1p, Sun1p, TBP1, and the 20S proteasome [8].
  • First, overexpression of two components of the 19 S RP, namely Pad1/Rpn11 and Mts3/Rpn12, rescued the temperature-sensitive growth defect of the dss1 mutant [9].
 

Analytical, diagnostic and therapeutic context of RPN12

References

  1. Cytokinin growth responses in Arabidopsis involve the 26S proteasome subunit RPN12. Smalle, J., Kurepa, J., Yang, P., Babiychuk, E., Kushnir, S., Durski, A., Vierstra, R.D. Plant Cell (2002) [Pubmed]
  2. Functional characterization of rpn3 uncovers a distinct 19S proteasomal subunit requirement for ubiquitin-dependent proteolysis of cell cycle regulatory proteins in budding yeast. Bailly, E., Reed, S.I. Mol. Cell. Biol. (1999) [Pubmed]
  3. CDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p. Yokota, K., Kagawa, S., Shimizu, Y., Akioka, H., Tsurumi, C., Noda, C., Fujimuro, M., Yokosawa, H., Fujiwara, T., Takahashi, E., Ohba, M., Yamasaki, M., DeMartino, G.N., Slaughter, C.A., Toh-e, A., Tanaka, K. Mol. Biol. Cell (1996) [Pubmed]
  4. A conditional lethal mutant in the fission yeast 26 S protease subunit mts3+ is defective in metaphase to anaphase transition. Gordon, C., McGurk, G., Wallace, M., Hastie, N.D. J. Biol. Chem. (1996) [Pubmed]
  5. Genetic evidence for interaction between components of the yeast 26S proteasome: combination of a mutation in RPN12 (a lid component gene) with mutations in RPT1 (an ATPase gene) causes synthetic lethality. Takeuchi, J., Toh-e, A. Mol. Gen. Genet. (1999) [Pubmed]
  6. A new essential gene of Saccharomyces cerevisiae, a defect in it may result in instability of nucleus. Nisogi, H., Kominami, K., Tanaka, K., Toh-e, A. Exp. Cell Res. (1992) [Pubmed]
  7. Characterization of the function of the NIN1 gene product of Saccharomyces cerevisiae. Kominami, K., Toh-e, A. Exp. Cell Res. (1994) [Pubmed]
  8. Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae. Fujimuro, M., Tanaka, K., Yokosawa, H., Toh-e, A. FEBS Lett. (1998) [Pubmed]
  9. Fission yeast Dss1 associates with the proteasome and is required for efficient ubiquitin-dependent proteolysis. Jossé, L., Harley, M.E., Pires, I.M., Hughes, D.A. Biochem. J. (2006) [Pubmed]
 
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