메뉴 건너뛰기




Volumn 178, Issue 6, 1996, Pages 1712-1719

Mutations within the first LSGGQ motif of Ste6p cause defects in a-factor transport and mating in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; MATING HORMONE ALPHA FACTOR;

EID: 0029867564     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.6.1712-1719.1996     Document Type: Article
Times cited : (24)

References (51)
  • 1
    • 0026472873 scopus 로고
    • Trafic ATPases: A superfamily of transport proteins operating from Escherichia coli to humans
    • Ames, G. F.-L., C. S. Mimura, S. R. Holbrook, and V. Shyamala. 1992 Trafic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans. Adv. Enzymol. 65:1-47.
    • (1992) Adv. Enzymol. , vol.65 , pp. 1-47
    • Ames, G.F.-L.1    Mimura, C.S.2    Holbrook, S.R.3    Shyamala, V.4
  • 2
    • 0025033814 scopus 로고
    • Bacterial periplasmic permeases belong to a family of transport proteins operating from E. coli to human: Traffic ATPases
    • Ames, G. F.-L., C. S. Mimura, and V. Shyamala. 1990. Bacterial periplasmic permeases belong to a family of transport proteins operating from E. coli to human: traffic ATPases. FEMS Microbiol. Rev. 75:429-47.
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 429-447
    • Ames, G.F.-L.1    Mimura, C.S.2    Shyamala, V.3
  • 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
    • 0021215427 scopus 로고
    • Different structure-function relationships for α-factor-induced morphogenesis and agglutination in Saccharomyces cerevisiae
    • Baffi, R. A., P. Shenbagamurthi, K. Terrance, J. M. Becker, F. Naider, and P. N. Lipke. 1984. Different structure-function relationships for α-factor-induced morphogenesis and agglutination in Saccharomyces cerevisiae. J. Bacteriol. 158:1152-1156.
    • (1984) J. Bacteriol. , vol.158 , pp. 1152-1156
    • Baffi, R.A.1    Shenbagamurthi, P.2    Terrance, K.3    Becker, J.M.4    Naider, F.5    Lipke, P.N.6
  • 5
    • 0028117116 scopus 로고
    • Metabolic instability and constitutive endocytosis of Ste6p, the a-factor transporter of Saccharomyces cerevisiae
    • Berkower, C., D. Loayza, and S. Michaelis. 1994. Metabolic instability and constitutive endocytosis of Ste6p, 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
  • 6
    • 0026094617 scopus 로고
    • Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP binding cassette (ABC) protein superfamily
    • Berkower, C., and S. Michaelis. 1991. Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP binding cassette (ABC) protein superfamily. EMBO J. 10:3777-3785.
    • (1991) EMBO J. , vol.10 , pp. 3777-3785
    • Berkower, C.1    Michaelis, S.2
  • 7
    • 0003383950 scopus 로고
    • Structures of genes encoding precursors of the yeast peptide mating pheromone a-factor
    • M.-J. Gething (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Brake, A., C. Brenner, R. Najarian, P. Laybourn, and J. Merriweather. 1985. Structures of genes encoding precursors of the yeast peptide mating pheromone a-factor, p. 103-108. In M.-J. Gething (ed.), Current communications in molecular biology: protein transport and secretion. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1985) Current Communications in Molecular Biology: Protein Transport and Secretion , pp. 103-108
    • Brake, A.1    Brenner, C.2    Najarian, R.3    Laybourn, P.4    Merriweather, J.5
  • 8
    • 0028170588 scopus 로고
    • Molecular determinants of bioactivity of the Saccharomyces cerevisiae lipopeptide mating pheromone
    • Caldwell, G. A., S.-H. Wang, C.-B. Xue, Y. Jiang, H.-F. Lu, F. Naider, and J. M. Becker. 1994 Molecular determinants of bioactivity of the Saccharomyces cerevisiae lipopeptide mating pheromone. J. Biol. Chem. 269:19817-19826.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19817-19826
    • Caldwell, G.A.1    Wang, S.-H.2    Xue, C.-B.3    Jiang, Y.4    Lu, H.-F.5    Naider, F.6    Becker, J.M.7
  • 10
    • 0025310336 scopus 로고
    • A cluster of cystic fibrosis mutations in the first nucleotide binding fold of the cystic fibrosis conductance regulator protein
    • Cutting, G. R., L. M. Kasch, B. J. Rosenstein, J. Zielenski, L.-C. Tsui, S. E. Antonarakis, and H. H. Kazazian. 1990. A cluster of cystic fibrosis mutations in the first nucleotide binding fold of the cystic fibrosis conductance regulator protein. Nature (London) 346:366-369.
    • (1990) Nature (London) , vol.346 , pp. 366-369
    • Cutting, G.R.1    Kasch, L.M.2    Rosenstein, B.J.3    Zielenski, J.4    Tsui, L.-C.5    Antonarakis, S.E.6    Kazazian, H.H.7
  • 11
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 12
    • 9044233521 scopus 로고
    • Genes required for cell fusion during mating
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Elia, L., and L. Marsh. 1995. Genes required for cell fusion during mating. p. 21. In Cold Spring Harbor Yeast Cell Biology Meeting Abstracts. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1995) Cold Spring Harbor Yeast Cell Biology Meeting Abstracts , pp. 21
    • Elia, L.1    Marsh, L.2
  • 13
    • 0022590783 scopus 로고
    • The amino terminus of the yeast F1-ATPase β subunit precursor functions as a mitochondrial import signal
    • Emr, S. D., A. Vassarotti, J. Garrett, B. L. Geller, M. Takeda, and M. G. Douglas. 1986. The amino terminus of the yeast F1-ATPase β subunit precursor functions as a mitochondrial import signal. J. Cell Biol. 102:523-533.
    • (1986) J. Cell Biol. , vol.102 , pp. 523-533
    • Emr, S.D.1    Vassarotti, A.2    Garrett, J.3    Geller, B.L.4    Takeda, M.5    Douglas, M.G.6
  • 14
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Geitz, R. D., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Geitz, R.D.1    Sugino, A.2
  • 15
    • 0025912486 scopus 로고
    • Maturation and function of cystic fibrosis transmembrane conductance regulator variants bearing mutations in putative nucleotide-binding domains 1 and 2
    • Gregory, R. J., D. P. Rich, S. H. Cheng, D. W. Souza, S. Paul, P. Manavalan, M. P. Anderson, M. J. Welsh, and A. E. Smith. 1991. Maturation and function of cystic fibrosis transmembrane conductance regulator variants bearing mutations in putative nucleotide-binding domains 1 and 2. Mol Cell. Biol. 11:3886-3893.
    • (1991) Mol Cell. Biol. , vol.11 , pp. 3886-3893
    • Gregory, R.J.1    Rich, D.P.2    Cheng, S.H.3    Souza, D.W.4    Paul, S.5    Manavalan, P.6    Anderson, M.P.7    Welsh, M.J.8    Smith, A.E.9
  • 18
    • 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
  • 19
    • 0025598073 scopus 로고
    • Courtship in S. cerevisiae: Both cell types choose mating partners by responding to the strongest pheromone signal
    • Jackson, C. L., and L. H. Hartwell. 1990. Courtship in S. cerevisiae: both cell types choose mating partners by responding to the strongest pheromone signal. Cell 63:1039-1051.
    • (1990) Cell , vol.63 , pp. 1039-1051
    • Jackson, C.L.1    Hartwell, L.H.2
  • 20
    • 0025268898 scopus 로고
    • Courtship in Saccharomyces cerevisiae: An early cell-cell interaction during mating
    • Jackson, C. L., and L. H. Hartwell. 1990. Courtship in Saccharomyces cerevisiae: an early cell-cell interaction during mating. Mol. Cell. Biol. 10:2202-2213
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2202-2213
    • Jackson, C.L.1    Hartwell, L.H.2
  • 21
    • 0026052120 scopus 로고
    • S cerevisiae α pheromone receptors activate a novel signal transduction pathway for mating partner discrimination
    • Jackson, C. L., J. B. Konopka, and L. H. Hartwell. 1991. S cerevisiae α pheromone receptors activate a novel signal transduction pathway for mating partner discrimination. Cell 67:389-402.
    • (1991) Cell , vol.67 , pp. 389-402
    • Jackson, C.L.1    Konopka, J.B.2    Hartwell, L.H.3
  • 22
    • 0021282354 scopus 로고
    • Glycosylation and processing of prepro-α-factor through the yeast secretory pathway
    • Julius, D., R. Schekman, and J. Thorner. 1984. Glycosylation and processing of prepro-α-factor through the yeast secretory pathway. Cell 36:309-318.
    • (1984) Cell , vol.36 , pp. 309-318
    • Julius, D.1    Schekman, R.2    Thorner, J.3
  • 24
    • 0026073302 scopus 로고
    • High expression vectors with multiple cloning sites for construction of trpE fusion proteins
    • Koerner, T. J., J. E. Hill, A. M. Myers, and A. Tzagoloff. 1991. High expression vectors with multiple cloning sites for construction of trpE fusion proteins Methods Enzymol. 194:477-490.
    • (1991) Methods Enzymol. , vol.194 , pp. 477-490
    • Koerner, T.J.1    Hill, J.E.2    Myers, A.M.3    Tzagoloff, A.4
  • 25
    • 0028277963 scopus 로고
    • The ABC transporter Ste6 accumulates in the plasma membrane in a ubiquinated form in endocytosis mutants
    • Kolling, R., and C. P. Hollenberg. 1994. The ABC transporter Ste6 accumulates in the plasma membrane in a ubiquinated form in endocytosis mutants. EMBO J. 13:3261-3271
    • (1994) EMBO J. , vol.13 , pp. 3261-3271
    • Kolling, R.1    Hollenberg, C.P.2
  • 26
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kubler, E., and H. Riezman. 1993. Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J. 12:2855-2862.
    • (1993) EMBO J. , vol.12 , pp. 2855-2862
    • Kubler, E.1    Riezman, H.2
  • 27
    • 0027476107 scopus 로고
    • The a-factor transporter (STE6 gene product) and cell polarity in the yeast Saccharomyces cerevisiae
    • Kuchler, K., H. G. Dohlman, and J. Thorner. 1993. The a-factor transporter (STE6 gene product) and cell polarity in the yeast Saccharomyces cerevisiae. J. Cell Biol. 120:1203-1215.
    • (1993) J. Cell Biol. , vol.120 , pp. 1203-1215
    • Kuchler, K.1    Dohlman, H.G.2    Thorner, J.3
  • 28
    • 0024833061 scopus 로고
    • Saccharomyces cerevisiae STE6 gene product: A novel pathway for protein export in eukaryotic cells
    • Kuchler, K., R. Sterne, and J. Thorner. 1989 Saccharomyces 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.2    Thorner, J.3
  • 29
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 30
    • 0026637326 scopus 로고
    • Pheromone response in yeast
    • Kurjan, J. 1992. Pheromone response in yeast. Annu. Rev. Biochem. 61: 1097-1129
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1097-1129
    • Kurjan, J.1
  • 31
    • 0025860189 scopus 로고
    • Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone
    • Marcus, S., G. A. Caldwell, D. Miller, C.-B. Xue, F. Naider, and J. M. Becker. 1991. Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces 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
  • 32
    • 0026761601 scopus 로고
    • Substitutions in the Hydrophobic core of the α-factor receptor of Saccharomyces cerevisiae permit response to Saccharomyces kluyven α-factor and to antagonist
    • Marsh, L. 1992. Substitutions in the Hydrophobic core of the α-factor receptor of Saccharomyces cerevisiae permit response to Saccharomyces kluyven α-factor and to antagonist. Mol. Cell. Biol. 12:3959-3966.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3959-3966
    • Marsh, L.1
  • 33
    • 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 (London) 340:400-404.
    • (1989) Nature (London) , vol.340 , pp. 400-404
    • McGrath, J.P.1    Varshavsky, A.2
  • 34
    • 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
  • 35
    • 0003842951 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1992. A short course in bacterial genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1992) A Short Course in Bacterial Genetics
    • Miller, J.H.1
  • 36
    • 0026053770 scopus 로고
    • Structural model of the nucleotide-binding conserved component of periplasmic permeases
    • Mimura, C. S., S. R. Holbrook, and G. F.-L. Ames. 1991. Structural model of the nucleotide-binding conserved component of periplasmic permeases. Proc. Natl. Acad. Sci. USA 88:84-88.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 84-88
    • Mimura, C.S.1    Holbrook, S.R.2    Ames, G.F.-L.3
  • 37
    • 0017730006 scopus 로고
    • Regulation of mating in the cell cycle of Saccharomyces cerevisiae
    • Reid, B. J., and L. H. Hartwell. 1977. Regulation of mating in the cell cycle of Saccharomyces cerevisiae. J. Cell Biol. 75:355-365.
    • (1977) J. Cell Biol. , vol.75 , pp. 355-365
    • Reid, B.J.1    Hartwell, L.H.2
  • 39
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • Rothstein, R. J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202-209.
    • (1983) Methods Enzymol. , vol.101 , pp. 202-209
    • Rothstein, R.J.1
  • 41
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., P. R. Sibbald, and A. Wittinghofer. 1990. The P-loop - a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15:430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 42
    • 0027076554 scopus 로고
    • Protein prenylation: Genes, enzymes, targets, and functions
    • Schafer, W. R., and J. Rine. 1992. Protein prenylation: genes, enzymes, targets, and functions Annu. Rev. Genet. 26:209-237.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 209-237
    • Schafer, W.R.1    Rine, J.2
  • 43
    • 0025971103 scopus 로고
    • Assay of yeast mating function
    • Sprague, G. 1991. Assay of yeast mating function. Methods Enzymol. 194: 77-93.
    • (1991) Methods Enzymol. , vol.194 , pp. 77-93
    • Sprague, G.1
  • 44
    • 0019719619 scopus 로고
    • Control of yeast cell type by the mating type locus identification and control of expression of the a-specific gene BAR1
    • Sprague, G., and I. Herskowitz. 1981. Control of yeast cell type by the mating type locus identification and control of expression of the a-specific gene BAR1. J. Mol. Biol. 153:305-321.
    • (1981) J. Mol. Biol. , vol.153 , pp. 305-321
    • Sprague, G.1    Herskowitz, I.2
  • 45
    • 0001134626 scopus 로고
    • Pheromone response and signal transduction during the mating process of Saccharomyces cerevisae
    • E. Jones, J. R. Pringle, and J. R. Broach (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Sprague, G. F., and J. W. Thorner. 1992. Pheromone response and signal transduction during the mating process of Saccharomyces cerevisae, p. 657-744. In E. Jones, J. R. Pringle, and J. R. Broach (ed.), The molecular and cellular biology of the yeast Saccharomyces: gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1992) The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression , pp. 657-744
    • Sprague, G.F.1    Thorner, J.W.2
  • 48
    • 0027034365 scopus 로고
    • Mutations and sequence variations detected in the cystic fibrosis transmembrane conductance regulator (CFTR) gene: A report from the Cystic Fibrosis Genetic Analysis Consortium
    • Tsui, L.-C. 1992 Mutations and sequence variations detected in the cystic fibrosis transmembrane conductance regulator (CFTR) gene: a report from the Cystic Fibrosis Genetic Analysis Consortium. Hum. Mutat. 1:197-203.
    • (1992) Hum. Mutat. , vol.1 , pp. 197-203
    • Tsui, L.-C.1
  • 49
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 8:945-951.
    • (1982) EMBO J. , vol.8 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 50
    • 0021680533 scopus 로고
    • Negative regulation of STE6 gene expression by the α2 product of Saccharomyces cerevisiae
    • Wilson, K. L., and I. Herskowitz. 1984. Negative regulation of STE6 gene expression by the α2 product of Saccharomyces cerevisiae. Mol. Cell. Biol. 4:2420-2427.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2420-2427
    • Wilson, K.L.1    Herskowitz, I.2
  • 51
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.