The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

RCE1  -  Rce1p

Saccharomyces cerevisiae S288c

Synonyms: CAAX prenyl protease 2, PPSEP 2, Prenyl protein-specific endoprotease 2, RACE, Ras and A-factor-converting enzyme, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of RCE1

  • Both yeast and human RCE1 proteins were produced in Sf9 insect cells by infection with a recombinant baculovirus; membrane preparations derived from the infected Sf9 cells exhibited a high level of prenyl protease activity [1].

High impact information on RCE1


Biological context of RCE1

  • Neither rce1-null nor yor291w-null mutations affected PIO or the phenotype of spf1- or ste24-null mutants [5].
  • We identified a mouse gene (designated Rce1) that shares sequence homology with a yeast gene (RCE1) implicated in the proteolytic processing of Ras2p [6].
  • At least 15 copies of the conserved domain of the 1.9 kb RCE1 centromeric repeats, which are similar to the long terminal repeats (LTRs) of gypsy-type retrotransposon RIRE7, were dispersed mainly in 320 kb stretches next to RCS2 tandem clusters [7].
  • Both Afc1p and Rce1p were able to proteolyze a-factor with A, V, L, I, C, or M at the a(1) position, V, L, I, C, or M at the a(2) position, or any amino acid at the X position that was acceptable for prenylation of the cysteine [4].
  • We have identified a previously overlooked gene in C. elegans chromosome V, which codes for a 266-amino-acid protein (CeFACE-2) with 30% sequence identity to human FACE-2/Rce1 [8].

Associations of RCE1 with chemical compounds

  • Results from the protease inhibition studies and the site-directed mutagenesis suggest that Rce1p is a cysteine protease [9].
  • Our mutational studies of residues conserved between the orthologs indicate that an alanine substitution at His194 completely inactivates yeast Rce1p enzymatic activity, whereas a substitution at Glu156 or His248 results in marginal activity [10].

Enzymatic interactions of RCE1

  • Ste24p cleaves the carboxyl-terminal "-AAX" from the yeast mating pheromone a-factor, whereas Rce1p cleaves the -AAX from both a-factor and Ras2p [11].

Regulatory relationships of RCE1

  • Homologous expression of plasmid-encoded Saccharomyces cerevisiae RCE1 under the control of the GAL1 promoter gave a 370-fold increase in endoprotease activity over an uninduced control [9].

Other interactions of RCE1

  • Two genes in yeast encoding CaaX endoproteases, AFC1 and RCE1, have been identified [9].

Analytical, diagnostic and therapeutic context of RCE1

  • Yeast Rce1p was detected by Western blotting with a yRce1p antibody or with an anti-myc antibody to Rce1p bearing a C-terminal myc-epitope [9].
  • To determine the intracellular site(s) at which CAAX processing occurs, we have examined the localization of the CAAX proteases Rce1p and Ste24p by subcellular fractionation and indirect immunofluorescence [3].
  • Molecular cloning of endo-beta-D-1,4-glucanase genes, rce1, rce2, and rce3, from Rhizopus oryzae [12].


  1. Cloning and characterization of a mammalian prenyl protein-specific protease. Otto, J.C., Kim, E., Young, S.G., Casey, P.J. J. Biol. Chem. (1999) [Pubmed]
  2. Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Boyartchuk, V.L., Ashby, M.N., Rine, J. Science (1997) [Pubmed]
  3. Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage. Schmidt, W.K., Tam, A., Fujimura-Kamada, K., Michaelis, S. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  4. The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities. Trueblood, C.E., Boyartchuk, V.L., Picologlou, E.A., Rozema, D., Poulter, C.D., Rine, J. Mol. Cell. Biol. (2000) [Pubmed]
  5. Yeast genes controlling responses to topogenic signals in a model transmembrane protein. Tipper, D.J., Harley, C.A. Mol. Biol. Cell (2002) [Pubmed]
  6. Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells. Kim, E., Ambroziak, P., Otto, J.C., Taylor, B., Ashby, M., Shannon, K., Casey, P.J., Young, S.G. J. Biol. Chem. (1999) [Pubmed]
  7. The centromere composition of multiple repetitive sequences on rice chromosome 5. Nonomura, K., Kurata, N. Chromosoma (2001) [Pubmed]
  8. Identification, functional expression and enzymic analysis of two distinct CaaX proteases from Caenorhabditis elegans. Cadiñanos, J., Schmidt, W.K., Fueyo, A., Varela, I., López-Otín, C., Freije, J.M. Biochem. J. (2003) [Pubmed]
  9. Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p. Dolence, J.M., Steward, L.E., Dolence, E.K., Wong, D.H., Poulter, C.D. Biochemistry (2000) [Pubmed]
  10. Mutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residues. Plummer, L.J., Hildebrandt, E.R., Porter, S.B., Rogers, V.A., McCracken, J., Schmidt, W.K. J. Biol. Chem. (2006) [Pubmed]
  11. Biochemical studies of Zmpste24-deficient mice. Leung, G.K., Schmidt, W.K., Bergo, M.O., Gavino, B., Wong, D.H., Tam, A., Ashby, M.N., Michaelis, S., Young, S.G. J. Biol. Chem. (2001) [Pubmed]
  12. Molecular cloning of endo-beta-D-1,4-glucanase genes, rce1, rce2, and rce3, from Rhizopus oryzae. Moriya, T., Murashima, K., Nakane, A., Yanai, K., Sumida, N., Koga, J., Murakami, T., Kono, T. J. Bacteriol. (2003) [Pubmed]
WikiGenes - Universities