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Volumn 136, Issue 2, 1997, Pages 271-285

A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; METALLOPROTEINASE;

EID: 0031048991     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.136.2.271     Document Type: Article
Times cited : (135)

References (70)
  • 1
    • 0028879135 scopus 로고
    • Role of yeast insulin-degrading enzyme homologues in propheromone processing and bud site selection
    • Adames, N., K. Blundell, M.N. Ashby, and C. Boone. 1995. Role of yeast insulin-degrading enzyme homologues in propheromone processing and bud site selection. Science (Wash. DC). 270:464-467.
    • (1995) Science (Wash. DC) , vol.270 , pp. 464-467
    • Adames, N.1    Blundell, K.2    Ashby, M.N.3    Boone, C.4
  • 3
    • 0024279583 scopus 로고
    • Structure of Saccharomyces cerevisiae mating hormone a-factor. Identification of S-farnesyl cysteine as a structural component
    • Anderegg, R.J., R. Betz, S.A. Carr, J.W. Crabb, and W. Duntze. 1988. Structure of Saccharomyces 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
  • 4
    • 0026521412 scopus 로고
    • Endoproteolytic processing of a farnesylated peptide in vitro
    • Ashby, M.N., D.S. King, and J. Rine. 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
  • 5
    • 0028999661 scopus 로고
    • Ras and a-factor converting enzyme
    • Ashby, M.N., and J. Rine. 1995. Ras and a-factor converting enzyme. Methods Enzymol. 250:235-250.
    • (1995) Methods Enzymol. , vol.250 , pp. 235-250
    • Ashby, M.N.1    Rine, J.2
  • 7
    • 0028117116 scopus 로고
    • Metabolic instability and constitutive endocytosis of STE6, the a-factor transporter of Saccharomyces cerevisiae
    • Berkower, C., D. Loayza, and S. Michaelis. 1994. Metabolic instability and constitutive endocytosis of STE6, the a-factor transporter of Saccharomyces cerevisiae. Mol. Biol. Cell. 5:1185-1198.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 1185-1198
    • Berkower, C.1    Loayza, D.2    Michaelis, S.3
  • 9
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoroorotic acid resistance
    • Boeke, J.D., F. Lacroute, and G.R. Fink, 1984. A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoroorotic acid resistance. Mol. Gen. Genet. 197:345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    Lacroute, F.2    Fink, G.R.3
  • 10
    • 0028019887 scopus 로고
    • Access to dbEST is available through the World Wide Web
    • Boguski, M.S., C.M. Tolstoshev, and J.D.E. Bassett. 1994. Access to dbEST is available through the World Wide Web. Science (Wash. DC). 265:1993-1994.
    • (1994) Science (Wash. DC) , vol.265 , pp. 1993-1994
    • Boguski, M.S.1    Tolstoshev, C.M.2    Bassett, J.D.E.3
  • 12
    • 0003383950 scopus 로고
    • Structure of genes encoding precursors of the yeast peptide mating pheromone a-factor
    • M.J. Gething, editor. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Brake, A.J., C. Brenner, R. Najarian, P. Laybourn, and J. Merryweather. 1985. Structure of genes encoding precursors of the yeast peptide mating pheromone a-factor. In Protein Transport and Secretion. M.J. Gething, editor. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 103-108.
    • (1985) Protein Transport and Secretion , pp. 103-108
    • Brake, A.J.1    Brenner, C.2    Najarian, R.3    Laybourn, P.4    Merryweather, J.5
  • 14
    • 0028215472 scopus 로고
    • Large-scale analysis of gene expression, protein localization, and gene disruption in Saccharomyces cerevisiae
    • Burns, N., B. Grimwade, P.B. Ross-Madonald, E.-Y. Choi, K. Finberg, G.S. Roeder, and M. Snyder. 1994. Large-scale analysis of gene expression, protein localization, and gene disruption in Saccharomyces cerevisiae. Genes Dev. 8:1087-1105.
    • (1994) Genes Dev. , vol.8 , pp. 1087-1105
    • Burns, N.1    Grimwade, B.2    Ross-Madonald, P.B.3    Choi, E.-Y.4    Finberg, K.5    Roeder, G.S.6    Snyder, M.7
  • 16
    • 0031055072 scopus 로고    scopus 로고
    • Biogenesis of the Saccharomyces cerevisiae mating pheromone a-factor
    • Chen, P., S.K. Sapperstein, J.D. Choi, and S. Michaelis. 1997. Biogenesis of the Saccharomyces 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
  • 17
    • 0026328042 scopus 로고
    • Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferase
    • Chen, W.J., D.A. Andres, J.L. Goldstein, and M.S. Brown. 1991a. Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferase. Proc. Natl. Acad. Sci. USA. 88:11368-11372.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11368-11372
    • Chen, W.J.1    Andres, D.A.2    Goldstein, J.L.3    Brown, M.S.4
  • 18
    • 0025871919 scopus 로고
    • cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase. the counterpart of yeast
    • Chen, W.J., D.A. Andres, J.L. Goldstein, D.W. Russell, and M.S. Brown. 1991b. cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase. the counterpart of yeast DPR1/RAM1 Cell 66:327-334.
    • (1991) DPR1/RAM1 Cell , vol.66 , pp. 327-334
    • Chen, W.J.1    Andres, D.A.2    Goldstein, J.L.3    Russell, D.W.4    Brown, M.S.5
  • 19
    • 0025019539 scopus 로고
    • Stoichiometry of G protein subunits affects the Saccharomyces cerevisiae mating pheromone signal transduction pathway
    • Cole, G.M., D.E. Stone, and S.I. Reed. 1990. Stoichiometry of G protein subunits affects the Saccharomyces cerevisiae mating pheromone signal transduction pathway. Mol. Cell. Biol. 10:510-517.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 510-517
    • Cole, G.M.1    Stone, D.E.2    Reed, S.I.3
  • 20
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson, P., and F. Letourneur. 1994. Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science (Wash. DC). 263:1629-1631.
    • (1994) Science (Wash. DC) , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 21
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeast
    • Elble, R. 1992. A simple and efficient procedure for transformation of yeast. BioTechniques. 13:53-65.
    • (1992) BioTechniques , vol.13 , pp. 53-65
    • Elble, R.1
  • 23
    • 0028151340 scopus 로고
    • A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes
    • Fujita, A., C. Oka, Y. Arikawa, T. Katagai, A. Tonouchi, S. Kuhara, and Y. Misumi. 1994. A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes. Nature (Lond.). 372:567-570.
    • (1994) Nature (Lond.) , 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
  • 24
    • 0023838558 scopus 로고
    • Enzymes required for yeast prohormone processing
    • Fuller, R.S., R.E. Sterne, and J. Thorner. 1988. Enzymes required for yeast prohormone processing. Annu. Rev. Physiol. 50:345-362.
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 345-362
    • Fuller, R.S.1    Sterne, R.E.2    Thorner, J.3
  • 26
    • 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., P. Chen, S.-Y. Chen, K.L. Vancura, S. Michaelis, and S. Powers. 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    Chen, S.-Y.3    Vancura, K.L.4    Michaelis, S.5    Powers, S.6
  • 27
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., B. Krummel, and R.K. Saiki. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16:7351-7367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 28
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper, N.M. 1994. Families of zinc metalloproteases. FEBS Lett. 354:1-6.
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 29
    • 0025051169 scopus 로고
    • Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae
    • Hrycyna, C.A., and S. Clarke. 1990. Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae. Mol. Cell. Biol. 10:5071-5076.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5071-5076
    • Hrycyna, C.A.1    Clarke, S.2
  • 30
    • 0025764049 scopus 로고
    • The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins
    • Hrycyna, C.A., S.K. Sapperstein, S. Clarke, and S. Michaelis. 1991. The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins. EMBO (Eur. Mol. Biol. Organ.) J. 10:1699-1709.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 1699-1709
    • Hrycyna, C.A.1    Sapperstein, S.K.2    Clarke, S.3    Michaelis, S.4
  • 31
    • 0026779707 scopus 로고
    • Maturation of isoprenylated proteins in Saccharomyces cerevisiae
    • Hrycyna, C.A., and S. Clarke. 1992. Maturation of isoprenylated proteins in Saccharomyces cerevisiae. J. Biol. Chem. 267:10457-10464.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10457-10464
    • Hrycyna, C.A.1    Clarke, S.2
  • 32
    • 0029022640 scopus 로고
    • Use of the yeast STE14 methyitransferase, expressed as a TrpE-STE14 fusion protein in Escherichia coli, for in vitro carboxylmethylation of isoprenylated polypeptides
    • Hrycyna, C.A., S.J. Wait, P.S. Backlund, and S. Michaelis. 1995. Use of the yeast STE14 methyitransferase, expressed as a TrpE-STE14 fusion protein in Escherichia coli, for in vitro carboxylmethylation of isoprenylated polypeptides. Methods Enzymol. 250:251-256.
    • (1995) Methods Enzymol. , vol.250 , pp. 251-256
    • Hrycyna, C.A.1    Wait, S.J.2    Backlund, P.S.3    Michaelis, S.4
  • 33
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 34
    • 0025184422 scopus 로고
    • Identification of a consensus motif for the retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson, M.R., T. Nilsson, and P.A. Peterson. 1990. Identification of a consensus motif for the retention of transmembrane proteins in the endoplasmic reticulum. EMBO (Eur. Mol. Biol. Organ.) J. 9:3153-3162.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 35
    • 0027538121 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Jackson, M.R., T. Nilsson, and P.A. Peterson. 1993. Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol. 121:317-333.
    • (1993) J. Cell Biol. , vol.121 , pp. 317-333
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 36
    • 0026451216 scopus 로고
    • Families of metalloendopeptidases and their relationship
    • Jiang, W., and J.S. Bond. 1992. Families of metalloendopeptidases and their relationship. FEBS Lett. 242:110-114.
    • (1992) FEBS Lett. , vol.242 , pp. 110-114
    • Jiang, W.1    Bond, J.S.2
  • 37
    • 0024559146 scopus 로고
    • A unique signature identifies a family of zinc-dependent metallopeptidases
    • Jongeneel, C.V., J. Bouvier, and A. Bairoch. 1989. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 242:211-214.
    • (1989) FEBS Lett. , vol.242 , pp. 211-214
    • Jongeneel, C.V.1    Bouvier, J.2    Bairoch, A.3
  • 38
    • 0021713896 scopus 로고
    • Isolation of the putative structural gene for the lysine-arginine-cleaving endo-peptidase required for processing of yeast prepro-a-factor
    • Julius, D., A. Brake, L. Blair, R. Kunisawa, and J. Thorner. 1984. Isolation of the putative structural gene for the lysine-arginine-cleaving endo-peptidase required for processing of yeast prepro-a-factor. Cell. 37:1075-1089.
    • (1984) Cell , vol.37 , pp. 1075-1089
    • Julius, D.1    Brake, A.2    Blair, L.3    Kunisawa, R.4    Thorner, J.5
  • 39
    • 0025896449 scopus 로고
    • Isolation, characterization, and sequence of an Escherichia coli heat shock gene, htpx
    • Kornitzer, D., D. Teff, S. Altuvia, and A.B. Oppenheim. 1991. Isolation, characterization, and sequence of an Escherichia coli heat shock gene, htpx. J. Bacteriol. 173:2944-2953.
    • (1991) J. Bacteriol. , vol.173 , pp. 2944-2953
    • Kornitzer, D.1    Teff, D.2    Altuvia, S.3    Oppenheim, A.B.4
  • 40
    • 0024833061 scopus 로고
    • Saccharomyces cerevisiae STE6 gene product: A novel pathway for protein export in eukaryotic cells
    • Kuchler, K., R.E. Sterne, and J. Thorner. 1989. Saccharomyces cerevisiae STE6 gene product: a novel pathway for protein export in eukaryotic cells. EMBO (Eur. Mol. Biol. Organ.) J. 8:3973-3984.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 3973-3984
    • Kuchler, K.1    Sterne, R.E.2    Thorner, J.3
  • 41
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R.F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 43
    • 0015959499 scopus 로고
    • Mutations affecting sexual conjugation and related processes in Saccharomyces cerevisiae. I. Isolation and phenotypic characterization of nonmating mutants
    • MacKay, V., and T.R. Manney. 1974. Mutations affecting sexual conjugation and related processes in Saccharomyces cerevisiae. I. Isolation and phenotypic characterization of nonmating mutants. Genetics. 76:255-271.
    • (1974) Genetics , vol.76 , pp. 255-271
    • MacKay, V.1    Manney, T.R.2
  • 44
    • 0024375860 scopus 로고
    • The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein
    • McGrath, J.P., and A. Varshavsky. 1989. The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein. Nature (Lond.). 340:400-404.
    • (1989) Nature (Lond.) , vol.340 , pp. 400-404
    • McGrath, J.P.1    Varshavsky, A.2
  • 46
    • 0027546252 scopus 로고
    • STE6, the yeast a-factor transporter
    • Michaelis, S. 1993. STE6, the yeast a-factor transporter. Semin. Cell Biol. 4:17-27.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 17-27
    • Michaelis, S.1
  • 47
    • 0023974052 scopus 로고
    • The a-factor pheromone of Saccharomyces cerevisiae is essential for mating
    • Michaelis, S., and I. Herskowitz, 1988. The a-factor pheromone of Saccharomyces 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
  • 48
    • 0029283796 scopus 로고
    • Pheromone communication in the fission yeast Schizosaccharomyces pombe
    • Nielsen, O., and J. Davey. 1995. Pheromone communication in the fission yeast Schizosaccharomyces pombe. Semin. Cell Biol. 6:95-104.
    • (1995) Semin. Cell Biol. , vol.6 , pp. 95-104
    • Nielsen, O.1    Davey, J.2
  • 50
    • 0028044785 scopus 로고
    • Characterization of a plasma membrane-associated prenylcysteme-directed alpha carboxyl methyltransferase in human neurophils
    • Pillinger, M.H., C. Volker, J.B. Stock, G. Weissmann, and M.R. Philips. 1994. Characterization of a plasma membrane-associated prenylcysteme-directed alpha carboxyl methyltransferase in human neurophils. J. Biol. Chem. 269:1485-1492.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1485-1492
    • Pillinger, M.H.1    Volker, C.2    Stock, J.B.3    Weissmann, G.4    Philips, M.R.5
  • 51
    • 0022994652 scopus 로고
    • RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone
    • Powers, S., S. Michaelis, D. Broek, S. Santa Anna, J. Field, I. Herskowitz, and M. Wigler. 1986. RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone. Cell. 47:413-422.
    • (1986) Cell , vol.47 , pp. 413-422
    • Powers, S.1    Michaelis, S.2    Broek, D.3    Santa Anna, S.4    Field, J.5    Herskowitz, I.6    Wigler, M.7
  • 52
    • 0025225363 scopus 로고
    • STE11 is a protein kinase required for cell-type-specific transcription and signal transduction in yeast
    • Rhodes, N., L. Connell, and B. Errede. 1990. STE11 is a protein kinase required for cell-type-specific transcription and signal transduction in yeast. Genes Dev. 4:1862-1874.
    • (1990) Genes Dev. , vol.4 , pp. 1862-1874
    • Rhodes, N.1    Connell, L.2    Errede, B.3
  • 55
    • 0028125792 scopus 로고
    • Nucleotide sequence of the yeast STE14 gene, which encodes the RAS and a-factor isoprenylcysteine methyltransferase, and demonstration of its essential role in a-factor export
    • Sapperstein, S., C. Berkower, and S. Michaelis. 1994. Nucleotide sequence of the yeast STE14 gene, which encodes the RAS and a-factor isoprenylcysteine 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
  • 57
    • 0028840671 scopus 로고
    • The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the ret1-1 mutation in alpha-COP
    • Schroder, S., F. Schimmoller, B. Singer-Kruger, and H. Riezman. 1995. The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the ret1-1 mutation in alpha-COP. J. Cell Biol. 131:895-912.
    • (1995) J. Cell Biol. , vol.131 , pp. 895-912
    • Schroder, S.1    Schimmoller, F.2    Singer-Kruger, B.3    Riezman, H.4
  • 58
    • 0028674393 scopus 로고
    • Pro-protein convertases of subtilisin/kexin family
    • Seidah, N.G., and M. Chretien. 1994. Pro-protein convertases of subtilisin/kexin family. Methods Enzymol. 244:175-188.
    • (1994) Methods Enzymol. , vol.244 , pp. 175-188
    • Seidah, N.G.1    Chretien, M.2
  • 59
    • 0029916795 scopus 로고    scopus 로고
    • cDNA structure, tissue distribution, and chromosomal localization of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases
    • Seidah, N.G., J. Hamelin, M. Mamarbachi, W. Dong, H. Tardos, M. Mbikay, M. Chretien, and R. Day. 1996. cDNA structure, tissue distribution, and chromosomal localization of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases. Proc. Natl. Acad. Sci. USA. 93:3388-3393.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3388-3393
    • Seidah, N.G.1    Hamelin, J.2    Mamarbachi, M.3    Dong, W.4    Tardos, H.5    Mbikay, M.6    Chretien, M.7    Day, R.8
  • 60
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 61
    • 0001134626 scopus 로고
    • Pheromone Response and Signal Transduction during the Mating Process of Saccharomyces cerevisiae
    • E.W. Jones, J.R. Pringle, and J.R. Broach, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sprague, G.F., and J.W. Thorner. 1992, Pheromone Response and Signal Transduction during the Mating Process of Saccharomyces cerevisiae. The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression. E.W. Jones, J.R. Pringle, and J.R. Broach, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 657-744.
    • (1992) The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression , pp. 657-744
    • Sprague, G.F.1    Thorner, J.W.2
  • 62
    • 0025971103 scopus 로고
    • Assay of yeast mating reaction
    • Sprague, J.G.F. 1991. Assay of yeast mating reaction. Methods Enzymol. 194:77-93.
    • (1991) Methods Enzymol. , vol.194 , pp. 77-93
    • Sprague, J.G.F.1
  • 63
    • 0025085582 scopus 로고
    • Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic farnesyl cysteine-containing peptide substrate
    • Stephenson, R.C., and S. Clarke. 1990. Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic farnesyl cysteine-containing peptide substrate. J. Biol. Chem. 265:16248-16254.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16248-16254
    • Stephenson, R.C.1    Clarke, S.2
  • 64
    • 0025870323 scopus 로고
    • Identifying the recognition unit for G protein methytation
    • Tan, E.W., D. Perez-Sala, F.J. Canada, and R.R. Rando. 1991. Identifying the recognition unit for G protein methytation. J. Biol. Chem. 266:10719-10722.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10719-10722
    • Tan, E.W.1    Perez-Sala, D.2    Canada, F.J.3    Rando, R.R.4
  • 66
    • 0030020360 scopus 로고    scopus 로고
    • Biochemical and functional analysis of the YME1 gene product, an ATP and zinc-dependent mitochondrial protease from S. cerevisiae
    • Weber, E.R., T. Hanekamp, and P.E. Thorsness. 1996. Biochemical and functional analysis of the YME1 gene product, an ATP and zinc-dependent mitochondrial protease from S. cerevisiae. Mol. Biol. Cell. 7:307-317.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 307-317
    • Weber, E.R.1    Hanekamp, T.2    Thorsness, P.E.3
  • 67
    • 0025191033 scopus 로고
    • Overexpression of the STE4 gene leads to mating response in haploid Saccharomyces cerevisiae
    • Whiteway, M., L. Hougan, and D.Y. Thomas. 1990. Overexpression of the STE4 gene leads to mating response in haploid Saccharomyces cerevisiae. Mol. Cell. Biol. 10:217-222.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 217-222
    • Whiteway, M.1    Hougan, L.2    Thomas, D.Y.3
  • 68
    • 0023142339 scopus 로고
    • STE16, a new gene required for pheromone production by a cells of Saccharomyces cerevisiae
    • Wilson, K., and I. Herskowitz. 1987. STE16, a new gene required for pheromone production by a cells of Saccharomyces cerevisiae. Genetics. 115:441-449.
    • (1987) Genetics , vol.115 , pp. 441-449
    • Wilson, K.1    Herskowitz, I.2
  • 70
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F.L., and P.J. Casey. 1996. Protein prenylation: molecular mechanisms and 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


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