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Volumn 9, Issue 1, 1998, Pages 19-30

The processing of yeast pheromones

Author keywords

Mating; Pheromone; Processing; Yeast

Indexed keywords

EUKARYOTA;

EID: 0031994807     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1997.0197     Document Type: Article
Times cited : (13)

References (114)
  • 1
    • 0027144459 scopus 로고
    • The pheromone response pathway in S. cerevisiae
    • Kurjan J (1993) The pheromone response pathway in S. cerevisiae. Ann Rev Genet 27:147-179
    • (1993) Ann Rev Genet , vol.27 , pp. 147-179
    • Kurjan, J.1
  • 2
    • 0028985079 scopus 로고
    • MAP kinase pathways in yeast: For mating and more
    • Herskowitz I (1995) MAP kinase pathways in yeast: for mating and more. Cell 80:187-197
    • (1995) Cell , vol.80 , pp. 187-197
    • Herskowitz, I.1
  • 3
    • 0029283796 scopus 로고
    • Pheromone communication in the fission yeast Sch. pombe
    • Nielsen O, Davey J (1995) Pheromone communication in the fission yeast Sch. pombe. Semin Cell Biol 6:95-104
    • (1995) Semin Cell Biol , vol.6 , pp. 95-104
    • Nielsen, O.1    Davey, J.2
  • 4
    • 0028097869 scopus 로고
    • The fission yeast mating pheromone P-factor: Its molecular structure, gene structure and physiological activities to induce gene expression and G1 arrest in the mating partner
    • Imai Y, Yamamoto M (1994) The fission yeast mating pheromone P-factor: its molecular structure, gene structure and physiological activities to induce gene expression and G1 arrest in the mating partner. Genes Dev 8:328-338
    • (1994) Genes Dev , vol.8 , pp. 328-338
    • Imai, Y.1    Yamamoto, M.2
  • 5
    • 0020365369 scopus 로고
    • Structure of a yeast pheromone gene (MFα): A putative α-factor precursor contains four tandem repeats of mature α-factor
    • Kurjan J, Herskowitz I (1982) Structure of a yeast pheromone gene (MFα): a putative α-factor precursor contains four tandem repeats of mature α-factor. Cell 30:933-943
    • (1982) Cell , vol.30 , pp. 933-943
    • Kurjan, J.1    Herskowitz, I.2
  • 7
    • 0023900108 scopus 로고
    • Prepro-α-factor has a cleavable signal sequence
    • Waters MG, Evans EA, Blobel G (1988) Prepro-α-factor has a cleavable signal sequence. J Biol Chem 263:6209-6214
    • (1988) J Biol Chem , vol.263 , pp. 6209-6214
    • Waters, M.G.1    Evans, E.A.2    Blobel, G.3
  • 8
    • 0028596117 scopus 로고
    • Isolation and characterisation of krp, a dibasic endopeptidase required for cell viability in the fission yeast Sch. pombe
    • Davey J, Davis K, Imai Y, Yamamoto M, Matthews G (1994) Isolation and characterisation of krp, a dibasic endopeptidase required for cell viability in the fission yeast Sch. pombe. EMBO J 13:5910-5921
    • (1994) EMBO J , vol.13 , pp. 5910-5921
    • Davey, J.1    Davis, K.2    Imai, Y.3    Yamamoto, M.4    Matthews, G.5
  • 9
    • 0027078415 scopus 로고
    • The new enzymology of precursor processing endoproteases
    • Steiner DF, Smeekens SP, Ohagi S, Chan SJ (1992) The new enzymology of precursor processing endoproteases. J Biol Chem 267:23435-23438
    • (1992) J Biol Chem , vol.267 , pp. 23435-23438
    • Steiner, D.F.1    Smeekens, S.P.2    Ohagi, S.3    Chan, S.J.4
  • 10
    • 14744293993 scopus 로고
    • Processing of protein precursors by a novel family of subtilisin-related mammalian endoproteases
    • Smeekens SP (1993) Processing of protein precursors by a novel family of subtilisin-related mammalian endoproteases. BioTechnolnology 11:182-186
    • (1993) BioTechnolnology , vol.11 , pp. 182-186
    • Smeekens, S.P.1
  • 11
    • 0017295312 scopus 로고
    • Two chromosomal genes required for killing expression in killer strains of S. cerevisiae
    • Wickner RB, Leibowitz MJ (1976) Two chromosomal genes required for killing expression in killer strains of S. cerevisiae. Genetics 82:429-442
    • (1976) Genetics , vol.82 , pp. 429-442
    • Wickner, R.B.1    Leibowitz, M.J.2
  • 12
    • 0000352990 scopus 로고
    • A chromosomal gene required for killer plasmid expression, mating and sporulation in S. cerevisiae
    • Leibowitz MJ, Wickner RW (1976) A chromosomal gene required for killer plasmid expression, mating and sporulation in S. cerevisiae. Proc Natl Acad Sci USA 73:2061-2065
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2061-2065
    • Leibowitz, M.J.1    Wickner, R.W.2
  • 13
    • 0020724122 scopus 로고
    • Yeast α-factor is processed from a larger precursor polypeptide: The essential role of a membrane-bound dipeptidyl aminopeptidase
    • Julius D, Blair L, Brake A, Sprague G, Thorner J (1983) Yeast α-factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase. Cell 32:839-852
    • (1983) Cell , vol.32 , pp. 839-852
    • Julius, D.1    Blair, L.2    Brake, A.3    Sprague, G.4    Thorner, J.5
  • 14
    • 0021713896 scopus 로고
    • Isolation of the putative structural gene for the Lys-Arg-cleaving endopeptidase required for processing of yeast pre-pro-α-factor
    • Julius D, Brake A, Blair LN, Kunisawa R, Thorner J (1984) Isolation of the putative structural gene for the Lys-Arg-cleaving endopeptidase required for processing of yeast pre-pro-α-factor. Cell 37:1075-1089
    • (1984) Cell , vol.37 , pp. 1075-1089
    • Julius, D.1    Brake, A.2    Blair, L.N.3    Kunisawa, R.4    Thorner, J.5
  • 15
    • 0027080272 scopus 로고
    • Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts golgi retention and results in default transport to the vacuole
    • Wilcox CA, Redding K, Wright R, Fuller RS (1992) Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole. Mol Biol Cell 3:1353-1371
    • (1992) Mol Biol Cell , vol.3 , pp. 1353-1371
    • Wilcox, C.A.1    Redding, K.2    Wright, R.3    Fuller, R.S.4
  • 16
    • 0028171094 scopus 로고
    • Clathrin-dependent localization of α1,3 mannosyl-transferase to the Golgi complex of S. cerevisiae
    • Graham TR, Seeger M, Payne GS, MacKay VL, Emr SD (1994) Clathrin-dependent localization of α1,3 mannosyl-transferase to the Golgi complex of S. cerevisiae. J Cell Biol 127:667-678
    • (1994) J Cell Biol , vol.127 , pp. 667-678
    • Graham, T.R.1    Seeger, M.2    Payne, G.S.3    MacKay, V.L.4    Emr, S.D.5
  • 17
    • 0025930734 scopus 로고
    • Posttranslational processing of the prohormone-cleaving Kex2 protease in the S. cerevisiae secretory pathway
    • Wilcox CA, Fuller RS (1991) Posttranslational processing of the prohormone-cleaving Kex2 protease in the S. cerevisiae secretory pathway. J Cell Biol 115:297-307
    • (1991) J Cell Biol , vol.115 , pp. 297-307
    • Wilcox, C.A.1    Fuller, R.S.2
  • 18
    • 0026532760 scopus 로고
    • Structural and enzymatic characterisation of a purified prohormone processing enzyme: Secreted, soluble Kex2 protease
    • Brenner C, Fuller RS (1992) Structural and enzymatic characterisation of a purified prohormone processing enzyme: secreted, soluble Kex2 protease. Proc Natl Acad Sci USA 89:922-926
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 922-926
    • Brenner, C.1    Fuller, R.S.2
  • 19
    • 0026576926 scopus 로고
    • The pro-region of the Kex2 endoprotease of S. cerevisiae is removed by self-processing
    • Germain D, Dumas F, Vernet T, Bourbonnais Y, Thomas DY, Boileau G (1992) The pro-region of the Kex2 endoprotease of S. cerevisiae is removed by self-processing. FEBS Lett 299:283-286
    • (1992) FEBS Lett , vol.299 , pp. 283-286
    • Germain, D.1    Dumas, F.2    Vernet, T.3    Bourbonnais, Y.4    Thomas, D.Y.5    Boileau, G.6
  • 20
    • 0028242912 scopus 로고
    • A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease
    • Gluschankof P, Fuller RS (1994) A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease. EMBO J 13:2280-2288
    • (1994) EMBO J , vol.13 , pp. 2280-2288
    • Gluschankof, P.1    Fuller, R.S.2
  • 21
    • 0031001304 scopus 로고    scopus 로고
    • Activation of furin endoprotease is a multiple-step process: Requirements for acidification and internal propeptide cleavage
    • Anderson ED, VanSlyke JK, Thulin CD, Jean F, Thomas G (1997) Activation of furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage. EMBO J 16:1508-1518
    • (1997) EMBO J , vol.16 , pp. 1508-1518
    • Anderson, E.D.1    VanSlyke, J.K.2    Thulin, C.D.3    Jean, F.4    Thomas, G.5
  • 22
    • 0027051404 scopus 로고
    • A mutant Kex2 enzyme with a C-terminal HDEL sequence releases correctly folded human insulin-like growth factor-1 from a precursor accumulated in the yeast endoplasmic reticulum
    • Chaudhuri B, Latham SE, Stephan C (1992) A mutant Kex2 enzyme with a C-terminal HDEL sequence releases correctly folded human insulin-like growth factor-1 from a precursor accumulated in the yeast endoplasmic reticulum. Eur J Biochem 210:811-822
    • (1992) Eur J Biochem , vol.210 , pp. 811-822
    • Chaudhuri, B.1    Latham, S.E.2    Stephan, C.3
  • 23
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of the furin proprotein convertase: Localisation to the TGN and recycling from the cell surface
    • Molloy SS, Thomas L, Van Slyke JK, Stenberg PE, Thomas G (1994) Intracellular trafficking and activation of the furin proprotein convertase: localisation to the TGN and recycling from the cell surface. EMBO J 13:18-33
    • (1994) EMBO J , vol.13 , pp. 18-33
    • Molloy, S.S.1    Thomas, L.2    Van Slyke, J.K.3    Stenberg, P.E.4    Thomas, G.5
  • 24
    • 0025394708 scopus 로고
    • A novel aspartyl protease allowing KEX2-independent MFα propheromone processing in yeast
    • Egel-Mitani M, Flygenring HP, Hansen MT (1990) A novel aspartyl protease allowing KEX2-independent MFα propheromone processing in yeast. Yeast 6:127-137
    • (1990) Yeast , vol.6 , pp. 127-137
    • Egel-Mitani, M.1    Flygenring, H.P.2    Hansen, M.T.3
  • 25
    • 0025886252 scopus 로고
    • Heterologous expression of peptide hormone precursors in the yeast S. cerevisiae. Evidence for a novel prohormone endoprotease with specificity for monobasic amino acids
    • Bourbonnais Y, Danoff A, Thomas DY, Shields D (1991) Heterologous expression of peptide hormone precursors in the yeast S. cerevisiae. Evidence for a novel prohormone endoprotease with specificity for monobasic amino acids. J Biol Chem 266:13203-13209
    • (1991) J Biol Chem , vol.266 , pp. 13203-13209
    • Bourbonnais, Y.1    Danoff, A.2    Thomas, D.Y.3    Shields, D.4
  • 26
    • 0027510253 scopus 로고
    • Isolation and characterisation of saccharomyces cerevisiae mutants defective in somatostatin expression: Cloning and functional role of a yeast gene encoding an aspartyl protease in precursor processing at monobasic cleavage sites
    • Bourbonnais Y, Ash J, Daigle M, Thomas DY (1993) Isolation and characterisation of Saccharomyces cerevisiae mutants defective in somatostatin expression: cloning and functional role of a yeast gene encoding an aspartyl protease in precursor processing at monobasic cleavage sites. EMBO J 12:285-294
    • (1993) EMBO J , vol.12 , pp. 285-294
    • Bourbonnais, Y.1    Ash, J.2    Daigle, M.3    Thomas, D.Y.4
  • 27
    • 0028848292 scopus 로고
    • Shared functions in vivo of a glycosyl-phosphatidylinositol-linked aspartyl protease, MKC7, and the proprotein processing protease KEX2 in yeast
    • Komano H, Fuller RS (1995) Shared functions in vivo of a glycosyl-phosphatidylinositol-linked aspartyl protease, MKC7, and the proprotein processing protease KEX2 in yeast. Proc Natl Acad Sci USA 92:10752-10756
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10752-10756
    • Komano, H.1    Fuller, R.S.2
  • 28
    • 0029972862 scopus 로고    scopus 로고
    • Yeast aspartic protease 3 (YAP3) prefers substrates with basic residues in the P2, P1 and P2′ positions
    • Ledgerwood EC, Brennan SO, Cawley NX, Loh YP, George PM (1996) Yeast aspartic protease 3 (YAP3) prefers substrates with basic residues in the P2, P1 and P2′ positions. FEBS Lett 383:67-71
    • (1996) FEBS Lett , vol.383 , pp. 67-71
    • Ledgerwood, E.C.1    Brennan, S.O.2    Cawley, N.X.3    Loh, Y.P.4    George, P.M.5
  • 29
    • 0029157811 scopus 로고
    • The yeast proprotein convertase encoded by YAP3 is a glycophosphatidylinositol-anchored protein that localises to the plasma membrane
    • Ash J, Dominguez M, Bergeron JJM, Thomas DY, Bourbonnais Y (1995) The yeast proprotein convertase encoded by YAP3 is a glycophosphatidylinositol-anchored protein that localises to the plasma membrane. J Biol Chem 270:20847-20854
    • (1995) J Biol Chem , vol.270 , pp. 20847-20854
    • Ash, J.1    Dominguez, M.2    Bergeron, J.J.M.3    Thomas, D.Y.4    Bourbonnais, Y.5
  • 30
    • 0030897065 scopus 로고    scopus 로고
    • Heterologous expression of human cholecystokinin in S. cerevisiae. Evidence for a lysine-specific endopeptidase in the yeast secretory pathway
    • Rourke IJ, Johnsen AH, Din N, Petersen JGL, Rehfeld JF (1997) Heterologous expression of human cholecystokinin in S. cerevisiae. Evidence for a lysine-specific endopeptidase in the yeast secretory pathway. J Biol Chem 272:9720-9727
    • (1997) J Biol Chem , vol.272 , pp. 9720-9727
    • Rourke, I.J.1    Johnsen, A.H.2    Din, N.3    Petersen, J.G.L.4    Rehfeld, J.F.5
  • 32
    • 0028091725 scopus 로고
    • Furin activates pseudomonas exotoxin-A by specific cleavage in vivo and in vitro
    • Inocencio NM, Moehring JM, Moehring TJ (1994) Furin activates pseudomonas exotoxin-A by specific cleavage in vivo and in vitro. J Biol Chem 269:31831-31835
    • (1994) J Biol Chem , vol.269 , pp. 31831-31835
    • Inocencio, N.M.1    Moehring, J.M.2    Moehring, T.J.3
  • 33
    • 0021842682 scopus 로고
    • Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles
    • Loh YP, Parish DC, Tuteja R (1985) Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles. J Biol Chem 260:7194-7205
    • (1985) J Biol Chem , vol.260 , pp. 7194-7205
    • Loh, Y.P.1    Parish, D.C.2    Tuteja, R.3
  • 34
    • 0024431704 scopus 로고
    • Generation of Lys-3-melanotropin from pro-opiomelanocortin by a bovine intermediate lobe secretory vesicle membrane-associated aspartic protease and purified POMC converting enzyme
    • Estivariz FE, Birch NP, Loh YP (1989) Generation of Lys-3-melanotropin from pro-opiomelanocortin by a bovine intermediate lobe secretory vesicle membrane-associated aspartic protease and purified POMC converting enzyme. J Biol Chem 264:17796-17801
    • (1989) J Biol Chem , vol.264 , pp. 17796-17801
    • Estivariz, F.E.1    Birch, N.P.2    Loh, Y.P.3
  • 35
    • 0025999852 scopus 로고
    • The anglerfish somatostatin-28-generating propeptide converting enzyme is an aspartyl protease
    • Mackin RB, Noe BD, Spiess J (1991) The anglerfish somatostatin-28-generating propeptide converting enzyme is an aspartyl protease. Endocrinology 129:1951-1957
    • (1991) Endocrinology , vol.129 , pp. 1951-1957
    • Mackin, R.B.1    Noe, B.D.2    Spiess, J.3
  • 36
    • 0029041261 scopus 로고
    • Processing enzymes of pepsin family: Yeast aspartic protease 3 and pro-opiomelanocortin converting enzyme
    • Loh YP, Cawley NX (1995) Processing enzymes of pepsin family: yeast aspartic protease 3 and pro-opiomelanocortin converting enzyme. Methods Enzymol 248:136-146
    • (1995) Methods Enzymol , vol.248 , pp. 136-146
    • Loh, Y.P.1    Cawley, N.X.2
  • 38
    • 0027208062 scopus 로고
    • Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem repeats, are related to each other, and PIR1 and PIR2 are required for tolerance to heat shock
    • Toh-e A, Yasunaga S, Nisogi H, Tanaka K, Oguchi T, Matsui Y (1993) Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem repeats, are related to each other, and PIR1 and PIR2 are required for tolerance to heat shock. Yeast 9:481-494
    • (1993) Yeast , vol.9 , pp. 481-494
    • Toh-e, A.1    Yasunaga, S.2    Nisogi, H.3    Tanaka, K.4    Oguchi, T.5    Matsui, Y.6
  • 39
    • 0025341613 scopus 로고
    • Processing of yeast exoglucanase (β-glucosidase) in a KEX2-dependent manner
    • Basco RD, Gimenez-Gallego G, Larriba G (1990) Processing of yeast exoglucanase (β-glucosidase) in a KEX2-dependent manner. FEBS Lett 268:99-102
    • (1990) FEBS Lett , vol.268 , pp. 99-102
    • Basco, R.D.1    Gimenez-Gallego, G.2    Larriba, G.3
  • 40
    • 0030773093 scopus 로고    scopus 로고
    • Proteolysis of Sxa2, a carboxypeptidase involved in pheromone adaptation in yeast
    • Ladds G, Davey J (1997) Proteolysis of Sxa2, a carboxypeptidase involved in pheromone adaptation in yeast. Biochem Soc Trans 25:446
    • (1997) Biochem Soc Trans , vol.25 , pp. 446
    • Ladds, G.1    Davey, J.2
  • 41
    • 0018788901 scopus 로고
    • S. cerevisiae killer expression mutant kex2 has altered secretory proteins and glycoproteins
    • Rogers DT, Saville D, Bussey H (1979) S. cerevisiae killer expression mutant kex2 has altered secretory proteins and glycoproteins. Biochem Biophys Res Commun 90:187-193
    • (1979) Biochem Biophys Res Commun , vol.90 , pp. 187-193
    • Rogers, D.T.1    Saville, D.2    Bussey, H.3
  • 42
    • 0024679301 scopus 로고
    • KEX2 mutations suppress RNA polymerase II mutants and alter the temperature range of yeast cell growth
    • Martin C, Young RA (1989) KEX2 mutations suppress RNA polymerase II mutants and alter the temperature range of yeast cell growth. Mol Cell Biol 9:2341-2349
    • (1989) Mol Cell Biol , vol.9 , pp. 2341-2349
    • Martin, C.1    Young, R.A.2
  • 43
    • 0028242191 scopus 로고
    • S. cerevisiae mutants sensitive to the antimalarial and antiarrhythmic drug, quinidine
    • Conklin DS, Culbertson MR, Kung C (1994) S. cerevisiae mutants sensitive to the antimalarial and antiarrhythmic drug, quinidine. FEMS Microbiol Lett 119:221-228
    • (1994) FEMS Microbiol Lett , vol.119 , pp. 221-228
    • Conklin, D.S.1    Culbertson, M.R.2    Kung, C.3
  • 44
    • 0023653256 scopus 로고
    • Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and α-factor precursor processing
    • Dmochowska A, Dignard D, Henning D, Thomas DY, Bussey H (1987) Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and α-factor precursor processing. Cell 50:573-584
    • (1987) Cell , vol.50 , pp. 573-584
    • Dmochowska, A.1    Dignard, D.2    Henning, D.3    Thomas, D.Y.4    Bussey, H.5
  • 45
    • 0024674424 scopus 로고
    • Characterisation of the yeast KEX1 gene product: A carboxypeptidase involved in processing secreted precursor proteins
    • Cooper A, Bussey H (1989) Characterisation of the yeast KEX1 gene product: A carboxypeptidase involved in processing secreted precursor proteins. Mol Cell Biol 9:2706-2714
    • (1989) Mol Cell Biol , vol.9 , pp. 2706-2714
    • Cooper, A.1    Bussey, H.2
  • 46
    • 0027953619 scopus 로고
    • Secretion, purification and characterization of a soluble form of the yeast KEX1-encoded protein from insect-cell cultures
    • Latchinian-Sadek L, Thomas DY (1994) Secretion, purification and characterization of a soluble form of the yeast KEX1-encoded protein from insect-cell cultures. Eur J Biochem 219:647-652
    • (1994) Eur J Biochem , vol.219 , pp. 647-652
    • Latchinian-Sadek, L.1    Thomas, D.Y.2
  • 47
    • 0027085824 scopus 로고
    • Yeast Kex1p is a Golgi-associated membrane protein: Deletions in cytoplasmic targeting domain result in mislocalisation to the vacuolar membrane
    • Cooper A, Bussey H (1992) Yeast Kex1p is a Golgi-associated membrane protein: deletions in cytoplasmic targeting domain result in mislocalisation to the vacuolar membrane. J Cell Biol 119:1459-1468
    • (1992) J Cell Biol , vol.119 , pp. 1459-1468
    • Cooper, A.1    Bussey, H.2
  • 48
    • 0026727566 scopus 로고
    • Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default path way
    • Roberts CJ, Nothwehr SF, Stevens TH (1992) Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default path way. J Cell Biol 119:69-83
    • (1992) J Cell Biol , vol.119 , pp. 69-83
    • Roberts, C.J.1    Nothwehr, S.F.2    Stevens, T.H.3
  • 49
    • 0027443775 scopus 로고
    • Immunoisolation of Kex2p-containing organelles from yeast demonstrates colocalisation of three processing proteinases to a single Golgi compartment
    • Bryant NJ, Boyd A (1993) Immunoisolation of Kex2p-containing organelles from yeast demonstrates colocalisation of three processing proteinases to a single Golgi compartment. J Cell Sci 106:815-822
    • (1993) J Cell Sci , vol.106 , pp. 815-822
    • Bryant, N.J.1    Boyd, A.2
  • 50
    • 0023812485 scopus 로고
    • Secretion of somatostatin by S. cerevisiae. Correct proteolytic processing of pro-α-factor-somatostatin hybrids requires the products of the KEX2 and STE13 genes
    • Bourbonnais Y, Bolin D, Shields D (1988) Secretion of somatostatin by S. cerevisiae. Correct proteolytic processing of pro-α-factor-somatostatin hybrids requires the products of the KEX2 and STE13 genes. J Biol Chem 263:15342-15347
    • (1988) J Biol Chem , vol.263 , pp. 15342-15347
    • Bourbonnais, Y.1    Bolin, D.2    Shields, D.3
  • 51
    • 84989078843 scopus 로고
    • Isolation and DNA sequence of the STE13 gene encoding dipeptidyl aminopeptidase
    • Anna-Arriola SS, Herskowitz I (1994) Isolation and DNA sequence of the STE13 gene encoding dipeptidyl aminopeptidase. Yeast 10:801-810
    • (1994) Yeast , vol.10 , pp. 801-810
    • Anna-Arriola, S.S.1    Herskowitz, I.2
  • 52
    • 0027204816 scopus 로고
    • Membrane protein retention in the yeast Golgi apparatus: Dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues
    • Nothwehr SF, Roberts CJ, Stevens TH (1993) Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues. J Cell Biol 121:1197-1209
    • (1993) J Cell Biol , vol.121 , pp. 1197-1209
    • Nothwehr, S.F.1    Roberts, C.J.2    Stevens, T.H.3
  • 53
    • 0031055434 scopus 로고    scopus 로고
    • Two separate signals act independently to localise a yeast late Golgi membrane protein through a combination of retrieval and retention
    • Bryant NJ, Stevens TH (1997) Two separate signals act independently to localise a yeast late Golgi membrane protein through a combination of retrieval and retention. J Cell Biol 136:287-297
    • (1997) J Cell Biol , vol.136 , pp. 287-297
    • Bryant, N.J.1    Stevens, T.H.2
  • 54
    • 0026587548 scopus 로고
    • Mating pheromones of the fission yeast Sch. pombe: Purification and structural characterisation of M-factor and isolation and structural characterisation of two genes encoding the pheromone
    • Davey J (1992) Mating pheromones of the fission yeast Sch. pombe: purification and structural characterisation of M-factor and isolation and structural characterisation of two genes encoding the pheromone. EMBO J 11:951-960
    • (1992) EMBO J , vol.11 , pp. 951-960
    • Davey, J.1
  • 55
    • 0024279583 scopus 로고
    • Structure of S. cerevisiae mating hormone a-factor. Identification of S-farnesyl cysteine as a structural component
    • Anderegg RJ, Betz R, Carr SA, Crabb JW, Duntze W (1988) Structure of S. cerevisiae mating hormone a-factor. Identification of S-farnesyl cysteine as a structural component. J Biol Chem 263:18236-18240
    • (1988) J Biol Chem , vol.263 , pp. 18236-18240
    • Anderegg, R.J.1    Betz, R.2    Carr, S.A.3    Crabb, J.W.4    Duntze, W.5
  • 56
    • 0028221222 scopus 로고
    • Analysis of the structural genes encoding the M-factor in fission yeast Sch. pombe: Identification of a third gene mfm3
    • Kjaerulff S, Davey J, Nielsen O (1994) Analysis of the structural genes encoding the M-factor in fission yeast Sch. pombe: identification of a third gene mfm3. Mol Cell Biol 14:3895-3905
    • (1994) Mol Cell Biol , vol.14 , pp. 3895-3905
    • Kjaerulff, S.1    Davey, J.2    Nielsen, O.3
  • 57
    • 0003383950 scopus 로고
    • The structure of genes encoding precursors of the yeast mating pheromone, a-factor
    • (Gething MJ, ed). Cold Spring Harbor Laboratory Press
    • Brake A, Brenner C, Najarian R, Laybourne P, Merryweather J (1985) The structure of genes encoding precursors of the yeast mating pheromone, a-factor. in Protein Transport and Secretion (Gething MJ, ed) pp 103-108. Cold Spring Harbor Laboratory Press
    • (1985) Protein Transport and Secretion , pp. 103-108
    • Brake, A.1    Brenner, C.2    Najarian, R.3    Laybourne, P.4    Merryweather, J.5
  • 58
    • 0023974052 scopus 로고
    • The a-factor pheromone of S. cerevisiae is essential for mating
    • Michaelis S, Herskowitz I (1988) The a-factor pheromone of S. cerevisiae is essential for mating. Mol Cell Biol 8:1309-1318
    • (1988) Mol Cell Biol , vol.8 , pp. 1309-1318
    • Michaelis, S.1    Herskowitz, I.2
  • 59
    • 0040222276 scopus 로고
    • Cloning of a gene coding for rhodotorucine a, a farnesyl peptide mating pheromone of R. toruloides
    • Akada R, Minomi K, Yamashita I, Miyakawa T, Fukui S (1987) Cloning of a gene coding for rhodotorucine A, a farnesyl peptide mating pheromone of R. toruloides. Agric Biol Chem 51:1211-1215
    • (1987) Agric Biol Chem , vol.51 , pp. 1211-1215
    • Akada, R.1    Minomi, K.2    Yamashita, I.3    Miyakawa, T.4    Fukui, S.5
  • 61
    • 0027479079 scopus 로고
    • The α-mating type locus of C. neoformans contains a peptide pheromone gene
    • Moore TDE, Edman JC (1993) The α-mating type locus of C. neoformans contains a peptide pheromone gene. Mol Cell Biol 13:1962-1970
    • (1993) Mol Cell Biol , vol.13 , pp. 1962-1970
    • Moore, T.D.E.1    Edman, J.C.2
  • 62
    • 0027076554 scopus 로고
    • Protein prenylation: Genes, enzymes, targets, and functions
    • Schafer WR, Rine JA (1992) Protein prenylation: genes, enzymes, targets, and functions. Ann Rev Genet 30:209-237
    • (1992) Ann Rev Genet , vol.30 , pp. 209-237
    • Schafer, W.R.1    Rine, J.A.2
  • 63
    • 0028232081 scopus 로고
    • Protein prenylation in eukaryotic microorganisms: Genetics, biology and biochemistry
    • Omer CA, Gibbs JB (1994) Protein prenylation in eukaryotic microorganisms: genetics, biology and biochemistry. Mol Microbiol 11:219-225
    • (1994) Mol Microbiol , vol.11 , pp. 219-225
    • Omer, C.A.1    Gibbs, J.B.2
  • 64
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanismsand functional consequences
    • Zhang FL, Casey PJ (1996) Protein prenylation: molecular mechanismsand functional consequences. Ann Rev Biochem 65:241-269
    • (1996) Ann Rev Biochem , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 65
    • 0026621245 scopus 로고
    • ABC transporters: Microorganisms to man
    • Higgins CF (1992) ABC transporters: microorganisms to man. Ann Rev Cell Biol 8:67-113
    • (1992) Ann Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 66
    • 0029586715 scopus 로고
    • Evolution of ATP-binding cassette transporter genes
    • Dean M, Allikmets R (1995) Evolution of ATP-binding cassette transporter genes. Curr Opin Gen Dev 5:779-785
    • (1995) Curr Opin Gen Dev , vol.5 , pp. 779-785
    • Dean, M.1    Allikmets, R.2
  • 67
    • 0024833061 scopus 로고
    • S. cerevisiae STE6 gene product. A novel pathway for protein export in eukaryotic cells
    • Kuchler K, Sterne RE, Thorner J (1989) S. cerevisiae STE6 gene product. A novel pathway for protein export in eukaryotic cells. EMBO J 8:3973-3984
    • (1989) EMBO J , vol.8 , pp. 3973-3984
    • Kuchler, K.1    Sterne, R.E.2    Thorner, J.3
  • 68
    • 0024375860 scopus 로고
    • The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein
    • McGrath JP, Varshavsky A (1989) The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein. Nature 340:400-404
    • (1989) Nature , vol.340 , pp. 400-404
    • McGrath, J.P.1    Varshavsky, A.2
  • 69
    • 0030797650 scopus 로고    scopus 로고
    • The Sch. pombe mam1 gene encodes an ABC transporter mediating secretion of M-factor
    • Christensen PU, Davey J, Nielsen O (1997) The Sch. pombe mam1 gene encodes an ABC transporter mediating secretion of M-factor. Mol Gen Genet 255:226-236
    • (1997) Mol Gen Genet , vol.255 , pp. 226-236
    • Christensen, P.U.1    Davey, J.2    Nielsen, O.3
  • 70
    • 0025830577 scopus 로고
    • C terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester
    • Farnsworth CC, Kawata M, Yoshida Y, Takai Y, Gelb MH, Glomset JA (1991) C terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester. Proc Natl Acad Sci USA 88:6196-6200
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6196-6200
    • Farnsworth, C.C.1    Kawata, M.2    Yoshida, Y.3    Takai, Y.4    Gelb, M.H.5    Glomset, J.A.6
  • 71
    • 0025787279 scopus 로고
    • Rab GTP-binding proteins implicated in vesicular transport are isoprenylated in vitro at cysteines within a novel carboxyl-terminal motif
    • Kinsella BT, Maltese WA(1991) Rab GTP-binding proteins implicated in vesicular transport are isoprenylated in vitro at cysteines within a novel carboxyl-terminal motif. J Biol Chem 266:8540-8544
    • (1991) J Biol Chem , vol.266 , pp. 8540-8544
    • Kinsella, B.T.1    Maltese, W.A.2
  • 72
    • 0025819073 scopus 로고
    • Protein farnesyltransferase and geranylgeranyltransferase share a common α-subunit
    • Seabra MC, Reiss Y, Casey PJ, Brown MS, Goldstein JL (1991) Protein farnesyltransferase and geranylgeranyltransferase share a common α-subunit. Cell 65:429-434
    • (1991) Cell , vol.65 , pp. 429-434
    • Seabra, M.C.1    Reiss, Y.2    Casey, P.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 74
    • 0026345033 scopus 로고
    • RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and ras proteins
    • He B, Chen P, Vancura KL, Michaelis S, Powers S (1991) RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins. Proc Natl Acad Sci USA 88:11373-11377
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11373-11377
    • He, B.1    Chen, P.2    Vancura, K.L.3    Michaelis, S.4    Powers, S.5
  • 75
    • 0022994652 scopus 로고
    • RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone a-factor
    • Powers S, Michaelis S, Brock D, Anna-Arriola SS, Field J, Herskowitz I, Wigler M (1986) RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone a-factor. Cell 47:413-422
    • (1986) Cell , vol.47 , pp. 413-422
    • Powers, S.1    Michaelis, S.2    Brock, D.3    Anna-Arriola, S.S.4    Field, J.5    Herskowitz, I.6    Wigler, M.7
  • 76
    • 0023081809 scopus 로고
    • A novel yeast mutant defective in the processing of ras proteins: Assessment of the effect of the mutation on processing steps
    • Fujiyama A, Matsumoto K, Tamanoi F (1987) A novel yeast mutant defective in the processing of ras proteins: assessment of the effect of the mutation on processing steps. EMBO J 6:223-228
    • (1987) EMBO J , vol.6 , pp. 223-228
    • Fujiyama, A.1    Matsumoto, K.2    Tamanoi, F.3
  • 77
    • 0024250829 scopus 로고
    • Structure and expression of yeast DPR1, a gene essential for the processing and intracellular localisation of ras proteins
    • Goodman LE, Perou CM, Fujiyama A, Tamanoi F (1988) Structure and expression of yeast DPR1, a gene essential for the processing and intracellular localisation of ras proteins. Yeast 4:271-281
    • (1988) Yeast , vol.4 , pp. 271-281
    • Goodman, L.E.1    Perou, C.M.2    Fujiyama, A.3    Tamanoi, F.4
  • 78
    • 0029972749 scopus 로고    scopus 로고
    • Enzymic characterisation of fission yeast farnesyl transferase. Recognition of the-CAAL motif at the C-terminus
    • Danjoh I, Fujiyama A (1996) Enzymic characterisation of fission yeast farnesyl transferase. Recognition of the-CAAL motif at the C-terminus. Eur J Biochem 236:847-851
    • (1996) Eur J Biochem , vol.236 , pp. 847-851
    • Danjoh, I.1    Fujiyama, A.2
  • 79
    • 0027375863 scopus 로고
    • The Sch. pombe cwg2 + gene codes for the β-subunit of a geranylgeranyltransferase type I required for β-glucan synthesis
    • Diaz M, Sanchez Y, Bennett T, Sun CR, Godoy C, Tamanoi F, Duran A, Perez P (1993) The Sch. pombe cwg2 + gene codes for the β-subunit of a geranylgeranyltransferase type I required for β-glucan synthesis. EMBO J 12:5245-5254
    • (1993) EMBO J , vol.12 , pp. 5245-5254
    • Diaz, M.1    Sanchez, Y.2    Bennett, T.3    Sun, C.R.4    Godoy, C.5    Tamanoi, F.6    Duran, A.7    Perez, P.8
  • 80
    • 0029819540 scopus 로고    scopus 로고
    • Isolation of ptb1, a gene for the β-subunit of a prenyltransferase from fission yeast
    • Godfrey R, Davey J (1996) Isolation of ptb1, a gene for the β-subunit of a prenyltransferase from fission yeast. Biochem Soc Trans 24:432
    • (1996) Biochem Soc Trans , vol.24 , pp. 432
    • Godfrey, R.1    Davey, J.2
  • 81
    • 0026521412 scopus 로고
    • Endoproteolytic processing of a farnesylated peptide in vitro
    • Ashby MN, King DS, Rine J (1992) Endoproteolytic processing of a farnesylated peptide in vitro. Proc Natl Acad Sci USA 89:4613-4617
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4613-4617
    • Ashby, M.N.1    King, D.S.2    Rine, J.3
  • 82
    • 0026779707 scopus 로고
    • Maturation of isoprenylated proteins in S. cerevisiae. Multiple activities catalyse the cleavage of the three carboxyl-terminal amino acids from farnesylated substrates in vitro
    • Hrycyna CA, Clarke S (1992) Maturation of isoprenylated proteins in S. cerevisiae. Multiple activities catalyse the cleavage of the three carboxyl-terminal amino acids from farnesylated substrates in vitro. J Biol Chem 267:10457-10464
    • (1992) J Biol Chem , vol.267 , pp. 10457-10464
    • Hrycyna, C.A.1    Clarke, S.2
  • 83
    • 0026680433 scopus 로고
    • A microsomal endoprotease that specifically cleaves isoprenylated peptides
    • Ma YT, Rando RR (1992) A microsomal endoprotease that specifically cleaves isoprenylated peptides. Proc Natl Acad Sci USA 89:6275-6279
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6275-6279
    • Ma, Y.T.1    Rando, R.R.2
  • 84
    • 0026454274 scopus 로고
    • Substrate specificity of the isoprenylated protein endoprotease
    • Ma YT, Chaudhuri A, Rando RR (1992) Substrate specificity of the isoprenylated protein endoprotease. Biochemistry 31:11772-11777
    • (1992) Biochemistry , vol.31 , pp. 11772-11777
    • Ma, Y.T.1    Chaudhuri, A.2    Rando, R.R.3
  • 85
    • 0028243621 scopus 로고
    • Proteolytic processing of farnesylated peptides: Assay and partial purification from pig brain membranes of an endopeptidase which has the characteristics of EC.3.4.24.15
    • Akopyan TN, Couedel Y, Orlowski M, Fournie-Zaluski MC, Roques BP (1994) Proteolytic processing of farnesylated peptides: assay and partial purification from pig brain membranes of an endopeptidase which has the characteristics of EC.3.4.24.15. Biochem Biophys Res Commun 198:787-794
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 787-794
    • Akopyan, T.N.1    Couedel, Y.2    Orlowski, M.3    Fournie-Zaluski, M.C.4    Roques, B.P.5
  • 86
    • 0030909336 scopus 로고    scopus 로고
    • Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
    • Boyartchuk VL, Ashby MN, Rine J (1997) Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science 275:1796-1800
    • (1997) Science , vol.275 , pp. 1796-1800
    • Boyartchuk, V.L.1    Ashby, M.N.2    Rine, J.3
  • 87
    • 0027479821 scopus 로고
    • Evolutionary families of peptidases
    • Rawlings ND, Barrett AJ (1993) Evolutionary families of peptidases. Biochem J 290:205-218
    • (1993) Biochem J , vol.290 , pp. 205-218
    • Rawlings, N.D.1    Barrett, A.J.2
  • 88
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson MR, Nilsson T, Peterson PA (1990) Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J 9:3153-3162
    • (1990) EMBO J , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 89
    • 0028029829 scopus 로고
    • Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast
    • Gaynor EC, Te Heesen S, Graham T, Aebi M, Emr SD (1994) Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast. J Cell Biol 127:653-665
    • (1994) J Cell Biol , vol.127 , pp. 653-665
    • Gaynor, E.C.1    Te Heesen, S.2    Graham, T.3    Aebi, M.4    Emr, S.D.5
  • 90
    • 0028840671 scopus 로고
    • The Golgi localisation of yeast EMP47p depends on its di-lysine motif but is not affected by the RET1-1 mutation in α-COP
    • Schroder S, Schimmoller F, Singerkruger B, Riezman H (1995) The Golgi localisation of yeast EMP47p depends on its di-lysine motif but is not affected by the RET1-1 mutation in α-COP. J Cell Biol 131:895-912
    • (1995) J Cell Biol , vol.131 , pp. 895-912
    • Schroder, S.1    Schimmoller, F.2    Singerkruger, B.3    Riezman, H.4
  • 91
    • 0031048991 scopus 로고    scopus 로고
    • A novel membrane-associated metalloprotease, Ste24p, is required for the first step of N-terminal processing of the yeast a-factor precursor
    • Fujimura-Kamada K, Nouvet FJ, Michaelis S (1997) A novel membrane-associated metalloprotease, Ste24p, is required for the first step of N-terminal processing of the yeast a-factor precursor. J Cell Biol 136:271-285
    • (1997) J Cell Biol , vol.136 , pp. 271-285
    • Fujimura-Kamada, K.1    Nouvet, F.J.2    Michaelis, S.3
  • 93
    • 0009680157 scopus 로고
    • Structures of Tremerogens A-9291-I and A-9291-VIII: Peptidyl sex hormones of T. brasiliensis
    • Ishibashi Y, Sakagami Y, Isogai A, Suzuki A (1984) Structures of Tremerogens A-9291-I and A-9291-VIII: Peptidyl sex hormones of T. brasiliensis. Biochemistry 23:1399-1404
    • (1984) Biochemistry , vol.23 , pp. 1399-1404
    • Ishibashi, Y.1    Sakagami, Y.2    Isogai, A.3    Suzuki, A.4
  • 94
    • 0025860189 scopus 로고
    • Significance of C-terminal cysteine modifications to the biological activity of the S. cerevisiae a-factor mating pheromone
    • Marcus S, Caldwell GA, Miller D, Xue C-B, Naider F, Becker JM (1991) Significance of C-terminal cysteine modifications to the biological activity of the S. cerevisiae a-factor mating pheromone. Mol Cell Biol 11:3603-3612
    • (1991) Mol Cell Biol , vol.11 , pp. 3603-3612
    • Marcus, S.1    Caldwell, G.A.2    Miller, D.3    Xue, C.-B.4    Naider, F.5    Becker, J.M.6
  • 95
    • 0025051169 scopus 로고
    • Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in S. cerevisiae
    • Hrycyna CA, Clarke S (1990) Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in S. cerevisiae. Mol Cell Biol 10:5071-5076
    • (1990) Mol Cell Biol , vol.10 , pp. 5071-5076
    • Hrycyna, C.A.1    Clarke, S.2
  • 96
    • 0025203977 scopus 로고
    • S. cerevisiae STE14 gene is required for COOH-terminal methylation of a-factor mating pheromone
    • Marr RS, Blair LC, Thorner J (1990) S. cerevisiae STE14 gene is required for COOH-terminal methylation of a-factor mating pheromone. J Biol Chem 265:20057-20060
    • (1990) J Biol Chem , vol.265 , pp. 20057-20060
    • Marr, R.S.1    Blair, L.C.2    Thorner, J.3
  • 97
    • 0025764049 scopus 로고
    • The S. cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins
    • Hrycyna CA, Sapperstein SK, Clarke S, Michaelis S (1991) The S. cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins. EMBO J 10:1699-1709
    • (1991) EMBO J , vol.10 , pp. 1699-1709
    • Hrycyna, C.A.1    Sapperstein, S.K.2    Clarke, S.3    Michaelis, S.4
  • 98
    • 0027209772 scopus 로고
    • Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine-carboxyl methyltransferase
    • Ashby MN, Errada PR, Boyartchuk VL, Rine J (1993) Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine-carboxyl methyltransferase. Yeast 9:907-913
    • (1993) Yeast , vol.9 , pp. 907-913
    • Ashby, M.N.1    Errada, P.R.2    Boyartchuk, V.L.3    Rine, J.4
  • 99
    • 0028125792 scopus 로고
    • Nucleotide sequence of the yeast STE14 gene, which encodes farnesyl-cysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export
    • Sapperstein S, Berkower C, Michaelis S (1994) Nucleotide sequence of the yeast STE14 gene, which encodes farnesyl-cysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export. Mol Cell Biol 14:1438-1449
    • (1994) Mol Cell Biol , vol.14 , pp. 1438-1449
    • Sapperstein, S.1    Berkower, C.2    Michaelis, S.3
  • 100
    • 0031020235 scopus 로고    scopus 로고
    • Genes encoding farnesyl cysteine carboxyl methyltransferase in Sch. pombe and X. laevis
    • Imai Y, Davey J, Kawagishi-Kobayashi M, Yamamoto M (1997) Genes encoding farnesyl cysteine carboxyl methyltransferase in Sch. pombe and X. laevis. Mol Cell Biol 17:1543-1551
    • (1997) Mol Cell Biol , vol.17 , pp. 1543-1551
    • Imai, Y.1    Davey, J.2    Kawagishi-Kobayashi, M.3    Yamamoto, M.4
  • 101
    • 0026348178 scopus 로고
    • A single activity carboxy methylates both farnesyl and geranyl-geranyl cysteine residues
    • Volker C, Lane P, Kwee C, Johnson M, Stock J (1991) A single activity carboxy methylates both farnesyl and geranyl-geranyl cysteine residues. FEBS Lett 295:189-194
    • (1991) FEBS Lett , vol.295 , pp. 189-194
    • Volker, C.1    Lane, P.2    Kwee, C.3    Johnson, M.4    Stock, J.5
  • 102
    • 0030976043 scopus 로고    scopus 로고
    • An amino terminal prosequence is required for efficient synthesis of S. cerevisiae a-factor
    • Quinby GE, Deschenes RJ (1997) An amino terminal prosequence is required for efficient synthesis of S. cerevisiae a-factor. Biochim Biophys Acta 1356:23-34
    • (1997) Biochim Biophys Acta , vol.1356 , pp. 23-34
    • Quinby, G.E.1    Deschenes, R.J.2
  • 103
    • 0031055072 scopus 로고    scopus 로고
    • Biogenesis of the S. cerevisiae mating pheromone a-factor
    • Chen P, Sapperstein SK, Choi JD, Michaelis S (1997) Biogenesis of the S. cerevisiae mating pheromone a-factor. J Cell Biol 136:251-269
    • (1997) J Cell Biol , vol.136 , pp. 251-269
    • Chen, P.1    Sapperstein, S.K.2    Choi, J.D.3    Michaelis, S.4
  • 104
    • 0028879135 scopus 로고
    • Role of yeast insulin-degrading enzyme homologsin prepheromone processing and bud site selection
    • Adames N, Blundell K, Ashby MN, Boone C (1995) Role of yeast insulin-degrading enzyme homologsin prepheromone processing and bud site selection. Science 270:464-467
    • (1995) Science , vol.270 , pp. 464-467
    • Adames, N.1    Blundell, K.2    Ashby, M.N.3    Boone, C.4
  • 105
    • 17444437608 scopus 로고    scopus 로고
    • Proteases involved in the maturation of the M-factor mating pheromone in fission yeast
    • Hughes M, Davey J (1997) Proteases involved in the maturation of the M-factor mating pheromone in fission yeast. Biochem Soc Trans 25:447
    • (1997) Biochem Soc Trans , vol.25 , pp. 447
    • Hughes, M.1    Davey, J.2
  • 106
    • 0029022718 scopus 로고
    • Insulysin and pitrilysin: Insulin-degrading enzymes of mammals and bacteria
    • Becker AB, Roth RA (1995) Insulysin and pitrilysin: insulin-degrading enzymes of mammals and bacteria. Methods Enzymol 248:693-703
    • (1995) Methods Enzymol , vol.248 , pp. 693-703
    • Becker, A.B.1    Roth, R.A.2
  • 109
    • 0028151340 scopus 로고
    • A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes
    • Fujita A, Oka C, Arikawa Y, Katagai T, Tonouchi A, Kuhara S, Misumi Y (1994) A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes. Nature 372:567-570
    • (1994) Nature , vol.372 , pp. 567-570
    • Fujita, A.1    Oka, C.2    Arikawa, Y.3    Katagai, T.4    Tonouchi, A.5    Kuhara, S.6    Misumi, Y.7
  • 110
    • 0026519161 scopus 로고
    • Sch. pombe sxa1 + and sxa2 + encode putative proteases involved in the mating response
    • Imai Y, Yamamoto M (1992) Sch. pombe sxa1 + and sxa2 + encode putative proteases involved in the mating response. Mol Cell Biol 12:1827-1834
    • (1992) Mol Cell Biol , vol.12 , pp. 1827-1834
    • Imai, Y.1    Yamamoto, M.2
  • 111
    • 0029865986 scopus 로고    scopus 로고
    • The sxa2-dependent inactivation of the P-factor mating pheromone in the fission yeast Sch. pombe
    • Ladds G, Rasmussen EM, Young T, Nielsen O, Davey J (1996) The sxa2-dependent inactivation of the P-factor mating pheromone in the fission yeast Sch. pombe. Mol Microbiol 20:35-42
    • (1996) Mol Microbiol , vol.20 , pp. 35-42
    • Ladds, G.1    Rasmussen, E.M.2    Young, T.3    Nielsen, O.4    Davey, J.5
  • 113
    • 0026099016 scopus 로고
    • Degradation of a-factor by a S. cerevisiae α-mating-type-specific endopeptidase: Evidence for a role in recovery of cells from G1 arrest
    • Marcus S, Xue C-B, Naider F, Becker JM (1991) Degradation of a-factor by a S. cerevisiae α-mating-type-specific endopeptidase: evidence for a role in recovery of cells from G1 arrest. Mol Cell Biol 11:1030-1039
    • (1991) Mol Cell Biol , vol.11 , pp. 1030-1039
    • Marcus, S.1    Xue, C.-B.2    Naider, F.3    Becker, J.M.4
  • 114
    • 0023322764 scopus 로고
    • 2+-dependent membrane peptidase involved in the signaling of mating pheromone in R. toruloides
    • 2+-dependent membrane peptidase involved in the signaling of mating pheromone in R. toruloides. J Bacteriol 169:1626-1631
    • (1987) J Bacteriol , vol.169 , pp. 1626-1631
    • Miyakawa, T.1    Kaji, M.2    Jeong, Y.K.3    Tsuchiya, E.4    Fukui, S.5


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