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Gene Review

PRC1  -  carboxypeptidase C PRC1

Saccharomyces cerevisiae S288c

Synonyms: CPY1, Carboxypeptidase Y, Carboxypeptidase YSCY, LBC1, YMR297W, ...
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High impact information on PRC1


Biological context of PRC1

  • To increase the production of CPY in Saccharomyces cerevisiae we have placed its coding region (PRC1) under control of the strongly regulated yeast GAL1 promoter on multicopy plasmids and introduced the constructs into vpl1 mutant strains [4].
  • These results suggest that SCM, although not a core component of PRC1, interacts and functions with PRC1 in gene silencing [5].
  • We purified a 58 kDa serine protease from culture-supernatant of Pichia pastoris and found that the NH2-terminal amino acid sequence of this protease is closely homologous to that of mature protein of Saccharomyces cerevisiae carboxypeptidase Y (CPY), which is encoded by the PRC1 gene [6].
  • The open reading frame of the P. pastoris PRC1 gene consists of 1569 bp encoding a protein of 523 amino acids [6].
  • We constructed hypoglycosylated CPY* variants containing one, two or three N-glycans in various combinations and studied their degradation kinetics [7].

Anatomical context of PRC1

  • Unlike the situation with a single copy of PRC1 in which newly synthesized CPY is efficiently localized to the vacuole, plasmid-directed overproduction results in secretion of greater than 50% of the protein as the precursor form [8].
  • Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species [9].

Associations of PRC1 with chemical compounds

  • In this study we analysed two new variants of the mutated yeast carboxypeptidase yscY, CPY*: a carboxy-terminal fusion protein of CPY* and pig liver esterase and a CPY* species carrying an additional glycosylation site at its carboxy-terminus [9].
  • Mutant CPY carries an Arg instead of a Gly residue in a highly conserved region, two positions distant from the active-site Ser [10].

Regulatory relationships of PRC1


Other interactions of PRC1

  • Both PEP4 or PRC1 gene disruptions resulted in a lower frequency of mitochondrial DNA escape [12].
  • The phenotypic lag in the expression of the carboxypeptidase Y deficiency is abolished by nonsense mutations in either PRC1, the structural gene for carboxypeptidase Y, or PRB1, the structural gene for proteinase B. Models to explain these observations are proposed [13].
  • Direct involvement of yscY and ysc alpha was confirmed by sequential disruption of their structural genes PRC1 and KEX1, respectively [14].
  • Complete import of CPY into the lumen of the ER requests a new targeting mechanism for retrograde transport of the malfolded enzyme through the Sec61 channel to occur [15].
  • High levels of CPY production were obtained by induction of the GAL1 promoter when the cells had left the exponential phase, resulting in a growth-phase-dependent CPY production similar to that of cells with PRC1 under the control of its own promoter [4].

Analytical, diagnostic and therapeutic context of PRC1


  1. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Hiller, M.M., Finger, A., Schweiger, M., Wolf, D.H. Science (1996) [Pubmed]
  2. PRC1: a human mitotic spindle-associated CDK substrate protein required for cytokinesis. Jiang, W., Jimenez, G., Wells, N.J., Hope, T.J., Wahl, G.M., Hunter, T., Fukunaga, R. Mol. Cell (1998) [Pubmed]
  3. Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids. Valls, L.A., Winther, J.R., Stevens, T.H. J. Cell Biol. (1990) [Pubmed]
  4. Regulated overproduction and secretion of yeast carboxypeptidase Y. Nielsen, T.L., Holmberg, S., Petersen, J.G. Appl. Microbiol. Biotechnol. (1990) [Pubmed]
  5. Requirement for sex comb on midleg protein interactions in Drosophila polycomb group repression. Peterson, A.J., Mallin, D.R., Francis, N.J., Ketel, C.S., Stamm, J., Voeller, R.K., Kingston, R.E., Simon, J.A. Genetics (2004) [Pubmed]
  6. Cloning and characterization of the Pichia pastoris PRC1 gene encoding carboxypeptidase Y. Ohi, H., Ohtani, W., Okazaki, N., Furuhata, N., Ohmura, T. Yeast (1996) [Pubmed]
  7. Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation. Kostova, Z., Wolf, D.H. J. Cell. Sci. (2005) [Pubmed]
  8. Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y. Stevens, T.H., Rothman, J.H., Payne, G.S., Schekman, R. J. Cell Biol. (1986) [Pubmed]
  9. Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. Plemper, R.K., Deak, P.M., Otto, R.T., Wolf, D.H. FEBS Lett. (1999) [Pubmed]
  10. Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Finger, A., Knop, M., Wolf, D.H. Eur. J. Biochem. (1993) [Pubmed]
  11. Maturation of vacuolar (lysosomal) enzymes in yeast: proteinase yscA and proteinase yscB are catalysts of the processing and activation event of carboxypeptidase yscY. Mechler, B., Müller, H., Wolf, D.H. EMBO J. (1987) [Pubmed]
  12. Escape of mitochondrial DNA to the nucleus in yme1 yeast is mediated by vacuolar-dependent turnover of abnormal mitochondrial compartments. Campbell, C.L., Thorsness, P.E. J. Cell. Sci. (1998) [Pubmed]
  13. Genetic properties of mutations at the PEP4 locus in Saccharomyces cerevisiae. Zubenko, G.S., Park, F.J., Jones, E.W. Genetics (1982) [Pubmed]
  14. C-terminal proteolytic degradation of recombinant desulfato-hirudin and its mutants in the yeast Saccharomyces cerevisiae. Heim, J., Takabayashi, K., Meyhack, B., Märki, W., Pohlig, G. Eur. J. Biochem. (1994) [Pubmed]
  15. Endoplasmic reticulum degradation. Reverse protein transport and its end in the proteasome. Plemper, R.K., Wolf, D.H. Mol. Biol. Rep. (1999) [Pubmed]
  16. Inactivation of carboxypeptidase Y by mutational removal of the putative essential histidyl residue. Bech, L.M., Breddam, K. Carlsberg Res. Commun. (1989) [Pubmed]
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