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Gene Review

RPN11  -  proteasome regulatory particle lid subunit...

Saccharomyces cerevisiae S288c

Synonyms: 26S proteasome regulatory subunit RPN11, MPR1, Protein MPR1, Ubiquitin carboxyl-terminal hydrolase RPN11, YFR004W
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Disease relevance of RPN11

  • Escherichia coli cells expressing ppr1(+), like ones expressing MPR1, were resistant to AZC and produced an AZC acetyltransferase [1].
  • The MPR1 gene coding sequence driven by two different constitutive promoters, with or without the 5'- and 3'-noncoding sequence from the MPR1 gene adjacent to the conventional NOS terminator, was transformed into tobacco ( Nicotiana tabacum L. cv. Xanthi) plants via Agrobacterium tumefaciens infection [2].

High impact information on RPN11

  • Yeast proteasomes contain two deubiquitinating enzymes, Ubp6 and Rpn11 [3].
  • We provide evidence that RPN11 functions downstream of RAS2, and show that mutation of two additional proteasome subunits results in identical phenotypes [4].
  • We show that RPN11, a gene encoding a subunit of the regulatory cap of the proteasome, is required for UV-stimulated activation of Gcn4p target genes, but is dispensable for their activation by the general control pathway [4].
  • Role of the yeast acetyltransferase Mpr1 in oxidative stress: regulation of oxygen reactive species caused by a toxic proline catabolism intermediate [5].
  • In contrast, overexpression of MPR1 leads to an increase in cell viability and a decrease in ROS level after oxidative treatments [5].

Biological context of RPN11

  • Nevertheless, these rpn11 mutants suppress the mitochondrial phenotypes associated with mpr1-1 by intragene complementation [6].
  • A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology [7].
  • We recently have discovered, on the chromosome of Saccharomyces cerevisiae Sigma1278b, a novel gene MPR1 required for the resistance of Sigma1278 background strains to toxic AZC [8].
  • Mpr1p was considered to be a member of the N-acetyltransferase superfamily based on the results of an Ala-scan mutagenesis through the highly conserved region involved in binding acetyl-CoA in members of the superfamily [8].
  • Gene expression and enzymatic analysis showed that the cloned Spa MPR1 gene encodes an L-azetidine-2-carboxylic acid acetyltransferase of 231 amino acids, which has 87% identity to the MPR1 protein [9].

Anatomical context of RPN11


Associations of RPN11 with chemical compounds


Other interactions of RPN11

  • STS1 also interacted with the second suppressor, RPN11, a subunit of the 26S proteasome, in the two-hybrid system [12].
  • CSN6 haploinsufficiency restored growth, whereas reduction of proteasome subunits RPN8 or RPN11 had no effect [13].
  • Recent studies have revealed that similar metalloprotease motifs--JAMMs--in the Rpn11 subunit of the 26S proteasome lid and in the Csn5 subunit of the COP9 signalosome are involved in deubiquitination and deneddylation, respectively [14].
  • 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 [15].

Analytical, diagnostic and therapeutic context of RPN11

  • Further, genomic PCR analysis showed that most of the S. cerevisiae complex spp. have the sequence highly homologous to the MPR1 gene [9].


  1. Characterization of novel acetyltransferases found in budding and fission yeasts that detoxify a proline analogue, azetidine-2-carboxylic acid. Nomura, M., Nakamori, S., Takagi, H. J. Biochem. (2003) [Pubmed]
  2. Expression of a novel yeast gene that detoxifies the proline analog azetidine-2-carboxylate confers resistance during tobacco seed germination, callus and shoot formation. Zhang, X.H., Takagi, H., Widholm, J.M. Plant Cell Rep. (2004) [Pubmed]
  3. Deubiquitinating enzyme ubp6 functions noncatalytically to delay proteasomal degradation. Hanna, J., Hathaway, N.A., Tone, Y., Crosas, B., Elsasser, S., Kirkpatrick, D.S., Leggett, D.S., Gygi, S.P., King, R.W., Finley, D. Cell (2006) [Pubmed]
  4. The proteasome regulates the UV-induced activation of the AP-1-like transcription factor Gcn4. Stitzel, M.L., Durso, R., Reese, J.C. Genes Dev. (2001) [Pubmed]
  5. Role of the yeast acetyltransferase Mpr1 in oxidative stress: regulation of oxygen reactive species caused by a toxic proline catabolism intermediate. Nomura, M., Takagi, H. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  6. Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domain. Rinaldi, T., Pick, E., Gambadoro, A., Zilli, S., Maytal-Kivity, V., Frontali, L., Glickman, M.H. Biochem. J. (2004) [Pubmed]
  7. A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology. Rinaldi, T., Ricci, C., Porro, D., Bolotin-Fukuhara, M., Frontali, L. Mol. Biol. Cell (1998) [Pubmed]
  8. A novel acetyltransferase found in Saccharomyces cerevisiae Sigma1278b that detoxifies a proline analogue, azetidine-2-carboxylic acid. Shichiri, M., Hoshikawa, C., Nakamori, S., Takagi, H. J. Biol. Chem. (2001) [Pubmed]
  9. Polymorphism of the MPR1 gene required for toxic proline analogue resistance in the Saccharomyces cerevisiae complex species. Kimura, Y., Nakamori, S., Takagi, H. Yeast (2002) [Pubmed]
  10. Mitochondrial effects of the pleiotropic proteasomal mutation mpr1/rpn11: uncoupling from cell cycle defects in extragenic revertants. Rinaldi, T., Ricordy, R., Bolotin-Fukuhara, M., Frontali, L. Gene (2002) [Pubmed]
  11. Saccharomyces cerevisiae sigma 1278b has novel genes of the N-acetyltransferase gene superfamily required for L-proline analogue resistance. Takagi, H., Shichiri, M., Takemura, M., Mohri, M., Nakamori, S. J. Bacteriol. (2000) [Pubmed]
  12. Evidence for separable functions of Srp1p, the yeast homolog of importin alpha (Karyopherin alpha): role for Srp1p and Sts1p in protein degradation. Tabb, M.M., Tongaonkar, P., Vu, L., Nomura, M. Mol. Cell. Biol. (2000) [Pubmed]
  13. Growth suppression induced by the TRC8 hereditary kidney cancer gene is dependent upon JAB1/CSN5. Gemmill, R.M., Lee, J.P., Chamovitz, D.A., Segal, D., Hooper, J.E., Drabkin, H.A. Oncogene (2005) [Pubmed]
  14. Ubiquitin system: JAMMing in the name of the lid. Berndt, C., Bech-Otschir, D., Dubiel, W., Seeger, M. Curr. Biol. (2002) [Pubmed]
  15. 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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