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RPT1  -  proteasome regulatory particle base...

Saccharomyces cerevisiae S288c

Synonyms: 26S protease regulatory subunit 7 homolog, CIM5, Protein CIM5, Tat-binding homolog 3, YKL145W, ...
 
 
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High impact information on RPT1

  • The fusion proteins glutathione S-transferase (GST)-Rad23 and Rad4-haemagglutinin (HA), and the proteasome subunits Cim3 and Cim5, cofractionate through consecutive chromatography steps [1].
  • An alpha subunit of the proteolytically active 20S core complex of the 26S proteasome, Pre6/YOL038w, as well as an ATPase-type subunit of the regulatory 19S cap complex, Cim5/YOL145w, were tagged with GFP [2].
  • The most divergent phenotype was that of the rpt1 mutant, which was strongly growth defective despite showing no general defect in protein turnover [3].
  • In addition, rpt1 was unique among the rpt mutants in displaying a G1 cell-cycle defect [3].
  • Furthermore, we showed that deletion of UBR2 exhibited a strong synthetic growth defect with a mutation in the Rpt1 proteasome subunit when Rpn4 was overexpressed [4].
 

Biological context of RPT1

  • 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].
 

Associations of RPT1 with chemical compounds

  • This changes amino acid 446 of the RPT1 product from alanine to valine [5].
  • Nob1p was found only in proteasomal fractions in a glycerol gradient centrifugation profile and immuno-coprecipitated with Rpt1, which is an ATPase component of the yeast proteasomes [6].
 

Physical interactions of RPT1

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

Regulatory relationships of RPT1

  • However, Ubc4 levels in the proteasome were reduced significantly in a strain that expressed a mutant Rpt1 subunit [7].
 

Other interactions of RPT1

References

  1. Rad23 links DNA repair to the ubiquitin/proteasome pathway. Schauber, C., Chen, L., Tongaonkar, P., Vega, I., Lambertson, D., Potts, W., Madura, K. Nature (1998) [Pubmed]
  2. Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast. Enenkel, C., Lehmann, A., Kloetzel, P.M. EMBO J. (1998) [Pubmed]
  3. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. Rubin, D.M., Glickman, M.H., Larsen, C.N., Dhruvakumar, S., Finley, D. EMBO J. (1998) [Pubmed]
  4. Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase. Wang, L., Mao, X., Ju, D., Xie, Y. J. Biol. Chem. (2004) [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. Nob1p, a new essential protein, associates with the 26S proteasome of growing saccharomyces cerevisiae cells. Tone, Y., Tanahashi, N., Tanaka, K., Fujimuro, M., Yokosawa, H., Toh-e, A. Gene (2000) [Pubmed]
  7. Saccharomyces cerevisiae Ub-conjugating enzyme Ubc4 binds the proteasome in the presence of translationally damaged proteins. Chuang, S.M., Madura, K. Genetics (2005) [Pubmed]
  8. The proteasomal ATPase complex is required for stress-induced transcription in yeast. Sulahian, R., Johnston, S.A., Kodadek, T. Nucleic Acids Res. (2006) [Pubmed]
 
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