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RPN2  -  proteasome regulatory particle base...

Saccharomyces cerevisiae S288c

Synonyms: 26S proteasome regulatory subunit RPN2, SEN3, YIL075C
 
 
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High impact information on RPN2

  • Further, we demonstrate that RPN4 is extremely short-lived (t(1/2) approximately 2 min), that it directly interacts with RPN2, a subunit of the 26S proteasome, and that rpn4Delta cells are perturbed in their cell cycle [1].
  • The 26S proteasome is also required; a mutation of SEN3/RPN2 (sen3-1), which encodes an essential regulatory subunit of the 26S proteasome, partially blocks 4-NQO-induced degradation of Rpb1 [2].
  • The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo [3].
  • Using a genetic selection for mutants with increased expression of Sen1-derived fusion proteins, we identified mutations in a novel gene, designated SEN3 [3].
  • SEN3 is essential and encodes a 945-residue protein with sequence similarity to a subunit of an activator of the 20S proteasome from bovine erythrocytes, called PA700 [3].
 

Biological context of RPN2

  • Disruption of the SEN3 did not affect cell viability, but led to temperature-sensitive growth [4].
  • The functional abnormality induced by SEN3 disruption differs considerably from various phenotypes shown by the nin1-1 mutation, suggesting that these two regulatory subunits of the 26S proteasome play distinct roles in the various processes mediated by the 26S proteasome [4].
  • The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin alphabeta and proteasome functions [5].
 

Associations of RPN2 with chemical compounds

  • CDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p [4].
  • Maintenance of SEN3 disruptant cells at the restrictive temperature resulted in a variety of cellular dysfunctions, including defects in proteolysis mediated by the ubiquitin pathway, in the N-end rule system, in the stress response upon cadmium exposure, and in nuclear protein transportation [4].
 

Other interactions of RPN2

  • The SEN3 also was identified in a synthetic lethal screen with the nin1-1 mutant, a temperature-sensitive mutant of NIN1 [4].
  • By cross-linking experiments, Rpn1 and Rpn2 were identified as Ubl-binding subunits [6].

References

  1. RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit. Xie, Y., Varshavsky, A. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  2. Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae. Beaudenon, S.L., Huacani, M.R., Wang, G., McDonnell, D.P., Huibregtse, J.M. Mol. Cell. Biol. (1999) [Pubmed]
  3. The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo. DeMarini, D.J., Papa, F.R., Swaminathan, S., Ursic, D., Rasmussen, T.P., Culbertson, M.R., Hochstrasser, M. Mol. Cell. Biol. (1995) [Pubmed]
  4. 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]
  5. The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin alphabeta and proteasome functions. Wendler, P., Lehmann, A., Janek, K., Baumgart, S., Enenkel, C. J. Biol. Chem. (2004) [Pubmed]
  6. Identification of ubiquitin-like protein-binding subunits of the 26S proteasome. Saeki, Y., Sone, T., Toh-e, A., Yokosawa, H. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
 
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