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Volumn 5, Issue 1, 2009, Pages 45-52

Transport and signaling via the amino acid binding site of the yeast Gap1 amino acid transceptor

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; AMINO ACID TRANSPORTER; CYSTEINE; PROTEIN GAP1; SERINE; UNCLASSIFIED DRUG; VALINE;

EID: 57749119180     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.132     Document Type: Article
Times cited : (67)

References (47)
  • 1
    • 0032080298 scopus 로고    scopus 로고
    • Glucose sensing and signaling by two glucose receptors in the yeast Saccharomyces cerevisiae
    • Ozcan, S., Dover, J. & Johnston, M. Glucose sensing and signaling by two glucose receptors in the yeast Saccharomyces cerevisiae. EMBO J. 17, 2566-2573 (1998).
    • (1998) EMBO J , vol.17 , pp. 2566-2573
    • Ozcan, S.1    Dover, J.2    Johnston, M.3
  • 2
    • 0031963197 scopus 로고    scopus 로고
    • The permease homologue Ssy1p controls the expression of amino acid and peptide transporter genes in Saccharomyces cerevisiae
    • Didion, T., Regenberg, B., Jorgensen, M.U., Kielland-Brandt, M.C. & Andersen, H.A. The permease homologue Ssy1p controls the expression of amino acid and peptide transporter genes in Saccharomyces cerevisiae. Mol. Microbiol. 27, 643-650 (1998).
    • (1998) Mol. Microbiol , vol.27 , pp. 643-650
    • Didion, T.1    Regenberg, B.2    Jorgensen, M.U.3    Kielland-Brandt, M.C.4    Andersen, H.A.5
  • 3
    • 0032962927 scopus 로고    scopus 로고
    • Amino acid signaling in Saccharomyces cerevisiae: A permease-like sensor of external amino acids and F-Box protein Grr1p are required for transcriptional induction of the AGP1 gene, which encodes a broad-specificity amino acid permease
    • Iraqui, I. et al. Amino acid signaling in Saccharomyces cerevisiae: a permease-like sensor of external amino acids and F-Box protein Grr1p are required for transcriptional induction of the AGP1 gene, which encodes a broad-specificity amino acid permease. Mol. Cell. Biol. 19, 989-1001 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , pp. 989-1001
    • Iraqui, I.1
  • 4
    • 0032778041 scopus 로고    scopus 로고
    • Ssy1p and Ptr3p are plasma membrane components of a yeast system that senses extracellular amino acids
    • Klasson, H., Fink, G.R. & Ljungdahl, P.O. Ssy1p and Ptr3p are plasma membrane components of a yeast system that senses extracellular amino acids. Mol. Cell. Biol. 19, 5405-5416 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , pp. 5405-5416
    • Klasson, H.1    Fink, G.R.2    Ljungdahl, P.O.3
  • 6
    • 17644386151 scopus 로고    scopus 로고
    • The Mep2p ammonium permease controls nitrogen starvation-induced filamentous growth in Candida albicans
    • Biswas, K. & Morschhauser, J. The Mep2p ammonium permease controls nitrogen starvation-induced filamentous growth in Candida albicans. Mol. Microbiol. 56, 649-669 (2005).
    • (2005) Mol. Microbiol , vol.56 , pp. 649-669
    • Biswas, K.1    Morschhauser, J.2
  • 7
    • 0032473497 scopus 로고    scopus 로고
    • The MEP2 ammonium permease regulates pseudohyphal differentiation in Saccharomyces cerevisiae
    • Lorenz, M.C. & Heitman, J. The MEP2 ammonium permease regulates pseudohyphal differentiation in Saccharomyces cerevisiae. EMBO J. 17, 1236-1247 (1998).
    • (1998) EMBO J , vol.17 , pp. 1236-1247
    • Lorenz, M.C.1    Heitman, J.2
  • 8
    • 34547124353 scopus 로고    scopus 로고
    • Distinct sensor pathways in the hierarchical control of SNAT2, a putative amino acid transceptor, by amino acid availability
    • Hyde, R., Cwiklinski, E.L., MacAulay, K., Taylor, P.M. & Hundal, H.S. Distinct sensor pathways in the hierarchical control of SNAT2, a putative amino acid transceptor, by amino acid availability. J. Biol. Chem. 282, 19788-19798 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 19788-19798
    • Hyde, R.1    Cwiklinski, E.L.2    MacAulay, K.3    Taylor, P.M.4    Hundal, H.S.5
  • 9
    • 21044440310 scopus 로고    scopus 로고
    • PAT-related amino acid transporters regulate growth via a novel mechanism that does not require bulk transport of amino acids
    • Goberdhan, D.C., Meredith, D., Boyd, C.A. & Wilson, C. PAT-related amino acid transporters regulate growth via a novel mechanism that does not require bulk transport of amino acids. Development 132, 2365-2375 (2005).
    • (2005) Development , vol.132 , pp. 2365-2375
    • Goberdhan, D.C.1    Meredith, D.2    Boyd, C.A.3    Wilson, C.4
  • 10
    • 0038682500 scopus 로고    scopus 로고
    • Amino acid transporters: Roles in amino acid sensing and signalling in animal cells
    • Hyde, R., Taylor, P.M. & Hundal, H.S. Amino acid transporters: roles in amino acid sensing and signalling in animal cells. Biochem. J. 373, 1-18 (2003).
    • (2003) Biochem. J , vol.373 , pp. 1-18
    • Hyde, R.1    Taylor, P.M.2    Hundal, H.S.3
  • 11
    • 0032720694 scopus 로고    scopus 로고
    • The dual function of sugar carriers. Transport and sugar sensing
    • Lalonde, S. et al. The dual function of sugar carriers. Transport and sugar sensing. Plant Cell 11, 707-726 (1999).
    • (1999) Plant Cell , vol.11 , pp. 707-726
    • Lalonde, S.1
  • 12
    • 0032835137 scopus 로고    scopus 로고
    • Novel sensing mechanisms and targets for the cAMP-protein kinase A pathway in the yeast Saccharomyces cerevisiae
    • Thevelein, J.M. & de Winde, J.H. Novel sensing mechanisms and targets for the cAMP-protein kinase A pathway in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 33, 904-918 (1999).
    • (1999) Mol. Microbiol , vol.33 , pp. 904-918
    • Thevelein, J.M.1    de Winde, J.H.2
  • 13
    • 20044372151 scopus 로고    scopus 로고
    • Nutrient sensing systems for rapid activation of the protein kinase A pathway in yeast
    • Thevelein, J.M. et al. Nutrient sensing systems for rapid activation of the protein kinase A pathway in yeast. Biochem. Soc. Trans. 33, 253-256 (2005).
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 253-256
    • Thevelein, J.M.1
  • 14
    • 0242437856 scopus 로고    scopus 로고
    • The Gap1 general amino acid permease acts as an amino acid sensor for activation of protein kinase A targets in the yeast Saccharomyces cerevisiae
    • Donaton, M.C. et al. The Gap1 general amino acid permease acts as an amino acid sensor for activation of protein kinase A targets in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 50, 911-929 (2003).
    • (2003) Mol. Microbiol , vol.50 , pp. 911-929
    • Donaton, M.C.1
  • 15
    • 33645047174 scopus 로고    scopus 로고
    • Ammonium permease-based sensing mechanism for rapid ammonium activation of the protein kinase A pathway in yeast
    • Van Nuland, A. et al. Ammonium permease-based sensing mechanism for rapid ammonium activation of the protein kinase A pathway in yeast. Mol. Microbiol. 59, 1485-1505 (2006).
    • (2006) Mol. Microbiol , vol.59 , pp. 1485-1505
    • Van Nuland, A.1
  • 16
    • 0037328986 scopus 로고    scopus 로고
    • Inorganic phosphate is sensed by specific phosphate carriers and acts in concert with glucose as a nutrient signal for activation of the protein kinase A pathway in the yeast Saccharomyces cerevisiae
    • Giots, F., Donaton, M.C. & Thevelein, J.M. Inorganic phosphate is sensed by specific phosphate carriers and acts in concert with glucose as a nutrient signal for activation of the protein kinase A pathway in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 47, 1163-1181 (2003).
    • (2003) Mol. Microbiol , vol.47 , pp. 1163-1181
    • Giots, F.1    Donaton, M.C.2    Thevelein, J.M.3
  • 17
    • 0020774482 scopus 로고
    • Inactivation-reactivation process and repression of permease formation regulate several ammonia-sensitive permeases in the yeast Saccharomyces cerevisiae
    • Grenson, M. Inactivation-reactivation process and repression of permease formation regulate several ammonia-sensitive permeases in the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 133, 135-139 (1983).
    • (1983) Eur. J. Biochem , vol.133 , pp. 135-139
    • Grenson, M.1
  • 18
    • 0030994642 scopus 로고    scopus 로고
    • A C-terminal di-leucine motif and nearby sequences are required for NH4(+)-induced inactivation and degradation of the general amino acid permease, Gap1p, of Saccharomyces cerevisiae
    • Hein, C. & Andre, B. A C-terminal di-leucine motif and nearby sequences are required for NH4(+)-induced inactivation and degradation of the general amino acid permease, Gap1p, of Saccharomyces cerevisiae. Mol. Microbiol. 24, 607-616 (1997).
    • (1997) Mol. Microbiol , vol.24 , pp. 607-616
    • Hein, C.1    Andre, B.2
  • 19
    • 0028876606 scopus 로고
    • Transcriptional and posttranslational regulation of the general amino acid permease of Saccharomyces cerevisiae
    • Stanbrough, M. & Magasanik, B. Transcriptional and posttranslational regulation of the general amino acid permease of Saccharomyces cerevisiae. J. Bacteriol. 177, 94-102 (1995).
    • (1995) J. Bacteriol , vol.177 , pp. 94-102
    • Stanbrough, M.1    Magasanik, B.2
  • 20
    • 0029586511 scopus 로고
    • An overview of membrane transport proteins in Saccharomyces cerevisiae
    • Andre, B. An overview of membrane transport proteins in Saccharomyces cerevisiae. Yeast 11, 1575-1611 (1995).
    • (1995) Yeast , vol.11 , pp. 1575-1611
    • Andre, B.1
  • 21
    • 0036495003 scopus 로고    scopus 로고
    • Conservation of amino acid transporters in fungi, plants and animals
    • Wipf, D. et al. Conservation of amino acid transporters in fungi, plants and animals. Trends Biochem. Sci. 27, 139-147 (2002).
    • (2002) Trends Biochem. Sci , vol.27 , pp. 139-147
    • Wipf, D.1
  • 22
    • 0034613185 scopus 로고    scopus 로고
    • A method for determining the in vivo topology of yeast polytopic membrane proteins demonstrates that Gap1p fully integrates into the membrane independently of Shr3p
    • Gilstring, C.F. & Ljungdahl, P.O. A method for determining the in vivo topology of yeast polytopic membrane proteins demonstrates that Gap1p fully integrates into the membrane independently of Shr3p. J. Biol. Chem. 275, 31488-31495 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 31488-31495
    • Gilstring, C.F.1    Ljungdahl, P.O.2
  • 23
    • 0032031494 scopus 로고    scopus 로고
    • Functional sensitivity of polar surfaces on transmembrane helix 8 and cytoplasmic loop 8-9 of the Escherichia coli GABA (4-aminobutyrate) transporter encoded by gabP: Mutagenic analysis of a consensus amphipathic region found in transporters from bacteria to mammals
    • Hu, L.A. & King, S.C. Functional sensitivity of polar surfaces on transmembrane helix 8 and cytoplasmic loop 8-9 of the Escherichia coli GABA (4-aminobutyrate) transporter encoded by gabP: mutagenic analysis of a consensus amphipathic region found in transporters from bacteria to mammals. Biochem. J. 330, 771-776 (1998).
    • (1998) Biochem. J , vol.330 , pp. 771-776
    • Hu, L.A.1    King, S.C.2
  • 24
    • 0346843111 scopus 로고    scopus 로고
    • Induction of substrate specificity shifts by placement of alanine insertions within the consensus amphipathic region of the Escherichia coli GABA (gamma-aminobutyric acid) transporter encoded by gabP
    • King, S.C., Hu, L.A. & Pugh, A. Induction of substrate specificity shifts by placement of alanine insertions within the consensus amphipathic region of the Escherichia coli GABA (gamma-aminobutyric acid) transporter encoded by gabP. Biochem. J. 376, 645-653 (2003).
    • (2003) Biochem. J , vol.376 , pp. 645-653
    • King, S.C.1    Hu, L.A.2    Pugh, A.3
  • 25
    • 33646397570 scopus 로고    scopus 로고
    • Competitive intra- and extracellular nutrient sensing by the transporter homologue Ssy1p
    • Wu, B. et al. Competitive intra- and extracellular nutrient sensing by the transporter homologue Ssy1p. J. Cell Biol. 173, 327-331 (2006).
    • (2006) J. Cell Biol , vol.173 , pp. 327-331
    • Wu, B.1
  • 26
    • 0024971494 scopus 로고
    • Purification and characterization of neutral trehalase from the yeast ABYS1 mutant
    • App, H. & Holzer, H. Purification and characterization of neutral trehalase from the yeast ABYS1 mutant. J. Biol. Chem. 264, 17583-17588 (1989).
    • (1989) J. Biol. Chem , vol.264 , pp. 17583-17588
    • App, H.1    Holzer, H.2
  • 27
    • 0027989473 scopus 로고
    • Activation of trehalase during growth induction by nitrogen sources in the yeast Saccharomyces cerevisiae depends on the free catalytic subunits of cAMP-dependent protein kinase, but not on functional Ras proteins
    • Durnez, P. et al. Activation of trehalase during growth induction by nitrogen sources in the yeast Saccharomyces cerevisiae depends on the free catalytic subunits of cAMP-dependent protein kinase, but not on functional Ras proteins. Yeast 10, 1049-1064 (1994).
    • (1994) Yeast , vol.10 , pp. 1049-1064
    • Durnez, P.1
  • 28
    • 0026713757 scopus 로고
    • Nutrient-induced activation of trehalase in nutrient-starved cells of the yeast Saccharomyces cerevisiae: CAMP is not involved as second messenger
    • Hirimburegama, K. et al. Nutrient-induced activation of trehalase in nutrient-starved cells of the yeast Saccharomyces cerevisiae: cAMP is not involved as second messenger. J. Gen. Microbiol. 138, 2035-2043 (1992).
    • (1992) J. Gen. Microbiol , vol.138 , pp. 2035-2043
    • Hirimburegama, K.1
  • 29
    • 0021112584 scopus 로고
    • Genetic and biochemical evidence that trehalase is a substrate of cAMP-dependent protein kinase in yeast
    • Uno, I., Matsumoto, K., Adachi, K. & Ishikawa, T. Genetic and biochemical evidence that trehalase is a substrate of cAMP-dependent protein kinase in yeast. J. Biol. Chem. 258, 10867-10872 (1983).
    • (1983) J. Biol. Chem , vol.258 , pp. 10867-10872
    • Uno, I.1    Matsumoto, K.2    Adachi, K.3    Ishikawa, T.4
  • 30
    • 0032896365 scopus 로고    scopus 로고
    • The PDE1-encoded low-affinity phosphodiesterase in the yeast Saccharomyces cerevisiae has a specific function in controlling agonist-induced cAMP signaling
    • Ma, P., Wera, S., Van Dijck, P. & Thevelein, J.M. The PDE1-encoded low-affinity phosphodiesterase in the yeast Saccharomyces cerevisiae has a specific function in controlling agonist-induced cAMP signaling. Mol. Biol. Cell 10, 91-104 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 91-104
    • Ma, P.1    Wera, S.2    Van Dijck, P.3    Thevelein, J.M.4
  • 31
    • 0024988790 scopus 로고
    • Glucose-induced hyperaccumulation of cyclic AMP and defective glucose repression in yeast strains with reduced activity of cyclic AMP-dependent protein kinase
    • Mbonyi, K., van Aelst, L., Arguelles, J.C., Jans, A.W. & Thevelein, J.M. Glucose-induced hyperaccumulation of cyclic AMP and defective glucose repression in yeast strains with reduced activity of cyclic AMP-dependent protein kinase. Mol. Cell. Biol. 10, 4518-4523 (1990).
    • (1990) Mol. Cell. Biol , vol.10 , pp. 4518-4523
    • Mbonyi, K.1    van Aelst, L.2    Arguelles, J.C.3    Jans, A.W.4    Thevelein, J.M.5
  • 32
    • 0035941266 scopus 로고    scopus 로고
    • The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast Gap1 permease
    • De Craene, J.O., Soetens, O. & Andre, B. The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast Gap1 permease. J. Biol. Chem. 276, 43939-43948 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 43939-43948
    • De Craene, J.O.1    Soetens, O.2    Andre, B.3
  • 33
    • 33749467954 scopus 로고    scopus 로고
    • Activity-dependent reversible inactivation of the general amino acid permease
    • Risinger, A.L., Cain, N.E., Chen, E.J. & Kaiser, C.A. Activity-dependent reversible inactivation of the general amino acid permease. Mol. Biol. Cell 17, 4411-4419 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4411-4419
    • Risinger, A.L.1    Cain, N.E.2    Chen, E.J.3    Kaiser, C.A.4
  • 34
    • 33745615846 scopus 로고    scopus 로고
    • Amino acids regulate retrieval of the yeast general amino acid permease from the vacuolar targeting pathway
    • Rubio-Texeira, M. & Kaiser, C.A. Amino acids regulate retrieval of the yeast general amino acid permease from the vacuolar targeting pathway. Mol. Biol. Cell 17, 3031-3050 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3031-3050
    • Rubio-Texeira, M.1    Kaiser, C.A.2
  • 35
    • 0031867271 scopus 로고    scopus 로고
    • Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae
    • Springael, J.Y. & Andre, B. Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae. Mol. Biol. Cell 9, 1253-1263 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1253-1263
    • Springael, J.Y.1    Andre, B.2
  • 36
    • 0014853512 scopus 로고
    • Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. IV. Evidence for a general amino acid permease
    • Grenson, M., Hou, C. & Crabeel, M. Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. IV. Evidence for a general amino acid permease. J. Bacteriol. 103, 770-777 (1970).
    • (1970) J. Bacteriol , vol.103 , pp. 770-777
    • Grenson, M.1    Hou, C.2    Crabeel, M.3
  • 37
    • 39849093575 scopus 로고    scopus 로고
    • Hyper- and hyporesponsive mutant forms of the Saccharomyces cerevisiae Ssy1 amino acid sensor
    • Poulsen, P., Gaber, R.F. & Kielland-Brandt, M.C. Hyper- and hyporesponsive mutant forms of the Saccharomyces cerevisiae Ssy1 amino acid sensor. Mol. Membr. Biol. 25, 164-176 (2008).
    • (2008) Mol. Membr. Biol , vol.25 , pp. 164-176
    • Poulsen, P.1    Gaber, R.F.2    Kielland-Brandt, M.C.3
  • 38
    • 0029864499 scopus 로고    scopus 로고
    • Two glucose transporters in Saccharomyces cerevisiae are glucose sensors that generate a signal for induction of gene expression
    • Ozcan, S., Dover, J., Rosenwald, A.G., Wolfl, S. & Johnston, M. Two glucose transporters in Saccharomyces cerevisiae are glucose sensors that generate a signal for induction of gene expression. Proc. Natl. Acad. Sci. USA 93, 12428-12432 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12428-12432
    • Ozcan, S.1    Dover, J.2    Rosenwald, A.G.3    Wolfl, S.4    Johnston, M.5
  • 39
    • 0036210602 scopus 로고    scopus 로고
    • Properties of the glucose-6-phosphate transporter from Chlamydia pneumoniae (HPTcp) and the glucose-6-phosphate sensor from Escherichia coli (UhpC)
    • Schwoppe, C., Winkler, H.H. & Neuhaus, H.E. Properties of the glucose-6-phosphate transporter from Chlamydia pneumoniae (HPTcp) and the glucose-6-phosphate sensor from Escherichia coli (UhpC). J. Bacteriol. 184, 2108-2115 (2002).
    • (2002) J. Bacteriol , vol.184 , pp. 2108-2115
    • Schwoppe, C.1    Winkler, H.H.2    Neuhaus, H.E.3
  • 40
    • 0344837749 scopus 로고    scopus 로고
    • Connection of transport and sensing by UhpC, the sensor for external glucose-6-phosphate in Escherichia coli
    • Schwoppe, C., Winkler, H.H. & Neuhaus, H.E. Connection of transport and sensing by UhpC, the sensor for external glucose-6-phosphate in Escherichia coli. Eur. J. Biochem. 270, 1450-1457 (2003).
    • (2003) Eur. J. Biochem , vol.270 , pp. 1450-1457
    • Schwoppe, C.1    Winkler, H.H.2    Neuhaus, H.E.3
  • 41
    • 48749106109 scopus 로고    scopus 로고
    • The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport
    • Faham, S. et al. The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport. Science 321, 810-814 (2008).
    • (2008) Science , vol.321 , pp. 810-814
    • Faham, S.1
  • 42
    • 34447256364 scopus 로고    scopus 로고
    • Conformational change in an MFS protein: MD simulations of LacY
    • Holyoake, J. & Sansom, M.S. Conformational change in an MFS protein: MD simulations of LacY. Structure 15, 873-884 (2007).
    • (2007) Structure , vol.15 , pp. 873-884
    • Holyoake, J.1    Sansom, M.S.2
  • 43
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters
    • Yamashita, A., Singh, S.K., Kawate, T., Jin, Y. & Gouaux, E. Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters. Nature 437, 215-223 (2005).
    • (2005) Nature , vol.437 , pp. 215-223
    • Yamashita, A.1    Singh, S.K.2    Kawate, T.3    Jin, Y.4    Gouaux, E.5
  • 44
    • 0014709197 scopus 로고
    • Mutations affecting the repressibility of arginine biosynthetic enzymes in Saccharomyces cerevisiae
    • Bechet, J., Greenson, M. & Wiame, J.M. Mutations affecting the repressibility of arginine biosynthetic enzymes in Saccharomyces cerevisiae. Eur. J. Biochem. 12, 31-39 (1970).
    • (1970) Eur. J. Biochem , vol.12 , pp. 31-39
    • Bechet, J.1    Greenson, M.2    Wiame, J.M.3
  • 45
    • 0025372080 scopus 로고
    • GAP1, the general amino acid permease gene of Saccharomyces cerevisiae. Nucleotide sequence, protein similarity with the other bakers yeast amino acid permeases, and nitrogen catabolite repression
    • Jauniaux, J.C. & Grenson, M. GAP1, the general amino acid permease gene of Saccharomyces cerevisiae. Nucleotide sequence, protein similarity with the other bakers yeast amino acid permeases, and nitrogen catabolite repression. Eur. J. Biochem. 190, 39-44 (1990).
    • (1990) Eur. J. Biochem , vol.190 , pp. 39-44
    • Jauniaux, J.C.1    Grenson, M.2
  • 46
    • 0025785410 scopus 로고
    • A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors
    • Bonneaud, N. et al. A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors. Yeast 7, 609-615 (1991).
    • (1991) Yeast , vol.7 , pp. 609-615
    • Bonneaud, N.1
  • 47
    • 0034696963 scopus 로고    scopus 로고
    • Stimulation of the yeast high osmolarity glycerol (HOG) pathway: Evidence for a signal generated by a change in turgor rather than by water stress
    • Tamas, M.J., Rep, M., Thevelein, J.M. & Hohmann, S. Stimulation of the yeast high osmolarity glycerol (HOG) pathway: evidence for a signal generated by a change in turgor rather than by water stress. FEBS Lett. 472, 159-165 (2000).
    • (2000) FEBS Lett , vol.472 , pp. 159-165
    • Tamas, M.J.1    Rep, M.2    Thevelein, J.M.3    Hohmann, S.4


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