AFC1 and RCE1: isoprenylated CAAX processing enzymes

Details AFC1 and RCE1: isoprenylated CAAX processing enzymes AFC1 and RCE1: isoprenylated CAAX processing enzymes

2006-04-18

2006-04-18

Prouty, Rebecca E. (Department: 1652)

Chemistry: molecular biology and microbiology

Animal cell, per se ; composition thereof; process of...

C435S320100, C435S183000, C435S252300, C435S224000, C435S069100, C435S023000, C536S023100, C536S023200, C530S350000

Reexamination Certificate

active

07029911

ABSTRACT:
Two genes which encode polypeptides that mediate post-prenylation processing steps in CAAX polypeptides such as Ras are provided. The two genes (AFC1 and RCE1) encode polypeptides that mediate the removal of the AAX tripeptide from the CAAX polypeptide following prenylation. The genes and encoded polypeptides provide assays for testing compounds for an effect on post-prenylation processing steps. A heat shock assay for assessing Ras activity is also provided.

REFERENCES:
patent: 4997767 (1991-03-01), Nozaki et al.
Rose, M. et al., GenBank Database, Accession No. Z49617, Oct. 6, 1995.
Sambrook, J. et al., Mol. Cloning, Cold Spring Harbor Press, pp. 16.3-16.16, 1989.
Lye, G. et al., Accession No. Z49260, GenBank Database, May 16, 1995.
Akopyan, T.N., et al., Cleavage of farnesylated COOH-terminal heptapeptide of mouse N-ras by brain microsomal membranes: evidence for a carboxypeptidase which specifically removes the COOH-terminal methionine. Biochem Biophys Res Commun, 1992. 187(3): p. 1336-42.
Akopyan, T.N., et al., Proteolytic processing of farnesylated peptides: assay and partial purification from pig brain membranes of an endopeptidase which has characteristics of E.C. 3.4.24.15. Biochem Biophys Res Commun, 1994. 198(2): p. 787-94.
Ashby, M.N., D.S. King, and J. Rine, Endoproteolytic processing of a farnesylated peptide in vitro. Proc Natl Acad Sci U S A, 1992. 89(10): p. 4613-7.
Ashby, M.N., et al., Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine: carboxyl methyltransferase. Yeast, 1993. 9(8): p. 907-13.
Ashby, M.N. and J. Rine, Ras and a-factor converting enzyme. Methods Enzymol, 1995. 250: p. 235-51.
Ashby, M.N., CaaX converting enzymes. Curr Opin Lipidol, 1998. 9(2): p. 99-102.
Auffray, C., et al., GenBank Accession No. Z43273, Nov. 11, 1994.
Boyartchuk, V.L., M.N. Ashby, and J. Rine, Modulation of Ras and a-factor function by carboxyl-terminal proteolysis Science, 1997. 275(5307): p. 1796-800.
Chen, Y., Y.T. Ma, and R.R. Rando, Solubilization, partial purification, and affinity labeling of the membrane-bound isoprenylated protein endoprotease. Biochemistry, 1996. 35(10): p. 3227-37.
Ding, J., et al., Farnesyl-L-cysteine analogs can inhibit or initiate superoxide release by human neutrophils. J Biol Chem, 1994. 269(24): p. 16837-44.
Dudler, T. and M.H. Gelb, Replacement of the H-Ras farnesyl group by lipid analogues: implications for downstream processing and effector activation in Xenopus oocytes. Biochemistry, 1997. 36(41): p. 12434-41.
Farh, L., D.A. Mitchell, and R.J. Deschenes, Farnesylation and proteolysis are sequential, but distinct steps in the CaaX box modification pathway. Arch Biochem Biophys, 1995. 318(1): p. 113-21.
Fujimura-Kamada, K., F.J. Nouvet, and S. Michaelis, A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor. J Cell Biol, 1997. 136(2): p. 271-85.
Georgopapadakou, N.H., et al., A radiometric assay for Ras-processing peptidase using an enzymatically radiolabeled peptide. Anal Biochem, 1994. 218(2): p. 273-7.
Giner, J.L. and R.R. Rando, Novel methyltransferase activity modifying the carboxy terminal bis(geranylgeranyl)-Cys-Ala-Cys structure of small GTP-binding proteins. Biochemistry, 1994. 33(50): p. 15116-23.
Gutierrez, L., et al., Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis. Embo J, 1989. 8(4): p. 1093-8.
Hancock, J.F., K. Cadwallader, and C.J. Marshall, Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B). Embo J, 1991. 10(3): p. 641-6.
Hancock, J.F., Reticulocyte lysate assay for in vitro translation and posttranslational modification of Ras proteins. Methods Enzymol, 1995. 255: p. 60-5.
Hiwasa, T., T. Sawada, and S. Sakiyama, Synergistic induction of anchorage-independent growth of NIH3T3 mouse fibroblasts by cysteine proteinase inhibitors and a tumor promoter. J Biol Chem, 1996. 271(16): p. 9181-4.
Hrycyna, C.A. and S. Clarke, Maturation of isoprenylated proteins inSaccharomyces cerevisiae. Multiple activities catalyze the cleavage of the three carboxyl-terminal amino acids from farnesylated substrates in vitro. J Biol Chem, 1992. 267(15): p. 10457-64.
Hrycyna, C.A. and S. Clarke, Purification and characterization of a novel metalloendopeptidase fromSaccharomyces cerevisiae. Biochemistry, 1993. 32(42): p. 11293-301.
Jang, G.F., K. Yokoyama, and M.H. Gelb, A prenylated protein-specific endoprotease in rat liver microsomes that produces a carboxyl-terminal tripeptide. Biochemistry, 1993. 32(36): p. 9500-7.
Jang, G.F. and M.H. Gelb, Substrate specificity of mammalian prenyl protein-specific endoprotease activity. Biochemistry, 1998. 37(13): p. 4473-81.
Kato, K., et al., Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity. Proc Natl Acad Sci U S A, 1992. 89(14): p. 6403-7.
Ma, Y.T., A. Chaudhuri, and R.R. Rando, Substrate specificity of the isoprenylated protein endoprotease. Biochemistry, 1992. 31(47): p. 11772-7.
Ma, Y.T. and R.R. Rando, A microsomal endoprotease that specifically cleaves isoprenylated peptides. Proc Natl Acad Sci U S A, 1992. 89(14): p. 6275-9.
Ma, Y.T., B.A. Gilbert, and R.R. Rando, Inhibitors of the isoprenylated protein endoprotease. Biochemistry, 1993. 32(9): p. 2386-93.
Ma, Y.T. and R.R. Rando, Endoproteolysis of non-CAAX-containing isoprenylated peptides. FEBS Lett, 1993. 332(1-2): p. 105-10.
Ma, Y.T., et al., Mechanistic studies on human platelet isoprenylated protein methyltransferase: farnesylcysteine analogs block platelet aggregation without inhibiting the methyltransferase. Biochemistry, 1994. 33(18): p. 5414-20.
Maura, M., et al., GenBank Accession No. W14344, Sep. 10, 1996.
Nishii, W., et al., Partial purification and characterization of a CAAX-motif-specific protease from bovine brain using a novel fluorometric assay. J. Biochem (Tokyo), 1997. 122(2): p. 402-8.
Parish, C.A., D.P. Brazil, and R.R. Rando, On the mechanism of the inhibition of transducin function by farnesylcysteine analogs. Biochemistry, 1997. 36(9): p. 2686-93.
Perez-Sala, D., et al., Analogs of farnesylcysteine induce apoptosis in HL-60 cells. FEBS Lett, 1998. 426(3): p. 319-24.
Powers, S., et al., “RAM, a Gene of Yeast Required for a Functional Modification of RAS Proteins and for Production of Mating Pheromone a-Factor,” cell, 1986, 47:413-422.
Rando, R.R. and Y.T. Ma, Isoprenylated protein endopeptidase. Methods Enzymol, 1994. 244: p. 632-9.
Schmidt, W.K., et al., Endoplasmic reticulum membrane localization of rce1p and ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage. Proc Natl Acad Sci U S A, 1998. 95(19): p. 11175-80.
Shi, Y.Q. and R.R. Rando, Kinetic mechanism of isoprenylated protein methyltransferase. J Biol Chem, 1992. 267(14): p. 9547-51.
Tam, A., et al., Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing. J Cell Biol, 1998. 142(3): p. 635-49.
Tan, E.W. and R.R. Rando, Identification of an isoprenylated cysteine methyl ester hydrolase activity in bovine rod outer segment membranes. Biochemistry, 1992. 31(24): p. 5572-8.
Fujiyama, A., et al., A novel yeast mutant defective in the processing of ras proteins: assessment of the effect of the mutation on processing steps, EMBO J., vol. 6, No. 1, p. 223-228.
Sass, P., et al., Cloning and Characterization of the high-affinity cAMP phosphodiesterase ofS. cerevisiae, PNAS USA, 1986, 83:9303-9307.

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