메뉴 건너뛰기




Volumn 56, Issue 5-6, 1999, Pages 415-426

Molecular mechanism of heme signaling in yeast: The transcriptional activator Hap1 serves as the key mediator

Author keywords

Hap1; Heme signaling; Oxygen sensing; Transcriptional regulation; Yeast Rox1

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; HEME; TRANSCRIPTION FACTOR;

EID: 0032729833     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050442     Document Type: Review
Times cited : (165)

References (99)
  • 1
    • 0028964123 scopus 로고
    • The oxygen sensor protein, Fixl, of Rhizobium meliloti. Role of histidine residues in heme binding, phosphorylation and signal transduction
    • 1 Monson E. K., Ditta G. S. and Helinski D. R. (1995) The oxygen sensor protein, FixL, of Rhizobium meliloti. Role of histidine residues in heme binding, phosphorylation and signal transduction. J. Biol. Chem. 270: 5243-5550
    • (1995) J. Biol. Chem. , vol.270 , pp. 5243-5550
    • Monson, E.K.1    Ditta, G.S.2    Helinski, D.R.3
  • 2
    • 0027403425 scopus 로고
    • The oxygen sensor Fixl of Rhizobium meliloti is a membrane protein containing four possible transmembrane segments
    • 2 Lois A. F., Ditta G. S. and Helinski D. R. (1993) The oxygen sensor FixL of Rhizobium meliloti is a membrane protein containing four possible transmembrane segments. J. Bacteriol. 175: 1103-1109
    • (1993) J. Bacteriol. , vol.175 , pp. 1103-1109
    • Lois, A.F.1    Ditta, G.S.2    Helinski, D.R.3
  • 3
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • 3 Gilles-Gonzalez M. A., Ditta G. S. and Helinski D. R. (1991) A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Nature 350: 170-172
    • (1991) Nature , vol.350 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 4
    • 0003051838 scopus 로고
    • Oxygen and catabolite regulation of hemoprotein biosynthesis in the yeast Saccharomyces cerevisiae
    • Caughey W. J. (ed.), Academic Press, New York
    • 4 Mattoon J., Lancashire W., Sanders H., Carvajal E., Malamud D., Braz G. et al. (1979) Oxygen and catabolite regulation of hemoprotein biosynthesis in the yeast Saccharomyces cerevisiae. In: Biosynthesis of Heme and Cholorophylls, pp. 421-435, Caughey W. J. (ed.), Academic Press, New York
    • (1979) Biosynthesis of Heme and Cholorophylls , pp. 421-435
    • Mattoon, J.1    Lancashire, W.2    Sanders, H.3    Carvajal, E.4    Malamud, D.5    Braz, G.6
  • 5
    • 0002634758 scopus 로고
    • Tetrapyrrole and heme biosynthesis in the yeast Sacchromyces cerevisiae
    • Dailey H. A. (ed.), Green, New York
    • 5 Labbe-Rois R. and Labbe P. (1990) Tetrapyrrole and heme biosynthesis in the yeast Sacchromyces cerevisiae. In: Biosynthesis of Heme and Cholorophylls, pp. 235-285, Dailey H. A. (ed.), Green, New York
    • (1990) Biosynthesis of Heme and Cholorophylls , pp. 235-285
    • Labbe-Rois, R.1    Labbe, P.2
  • 6
    • 0031019657 scopus 로고    scopus 로고
    • Regulation of hypoxic gene expression in yeast
    • 6 Zitomer R. S., Carrico P. and Deckert J. (1997) Regulation of hypoxic gene expression in yeast. Kidney Int. 51: 507-513
    • (1997) Kidney Int. , vol.51 , pp. 507-513
    • Zitomer, R.S.1    Carrico, P.2    Deckert, J.3
  • 7
    • 0026559542 scopus 로고
    • Regulation of gene expression by oxygen in Saccharomyces cerevisiae
    • 7 Zitomer R. S. and Lowry C. V. (1992) Regulation of gene expression by oxygen in Saccharomyces cerevisiae. Microbiol. Rev. 56: 1-11
    • (1992) Microbiol. Rev. , vol.56 , pp. 1-11
    • Zitomer, R.S.1    Lowry, C.V.2
  • 8
    • 0029842459 scopus 로고    scopus 로고
    • Oxygen sensing and molecular adaptation to hypoxia
    • 8 Bunn H. F. and Poyton R. O. (1996) Oxygen sensing and molecular adaptation to hypoxia. Physiol. Rev. 76: 839-885
    • (1996) Physiol. Rev. , vol.76 , pp. 839-885
    • Bunn, H.F.1    Poyton, R.O.2
  • 9
    • 0024273450 scopus 로고
    • Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein
    • 9 Goldberg M. A., Dunning S. P. and Bunn H. F. (1988) Regulation of the erythropoietin gene: evidence that the oxygen sensor is a heme protein. Science 242: 1412-1415
    • (1988) Science , vol.242 , pp. 1412-1415
    • Goldberg, M.A.1    Dunning, S.P.2    Bunn, H.F.3
  • 11
    • 0029960838 scopus 로고    scopus 로고
    • The role of heme in gene expression
    • 11 Sassa S. and Nagai T. (1996) The role of heme in gene expression. Int. J. Hematol. 63: 167-178
    • (1996) Int. J. Hematol. , vol.63 , pp. 167-178
    • Sassa, S.1    Nagai, T.2
  • 12
    • 0029821892 scopus 로고    scopus 로고
    • Novel effects of heme and heme-related compounds in biological systems
    • 12 Sassa S. (1996) Novel effects of heme and heme-related compounds in biological systems. Curr. Med. Chem. 3: 273-290
    • (1996) Curr. Med. Chem. , vol.3 , pp. 273-290
    • Sassa, S.1
  • 13
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase
    • 13 Chen J. J. and London I. M. (1995) Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase. Trends Biochem. Sci. 20: 105-108
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.J.1    London, I.M.2
  • 14
    • 0019795284 scopus 로고
    • Induction of hemoglobin accumulation in human K562 cells by hemin is reversible
    • 14 Dean A., Erard F., Schneider A. P. and Schechter A. N. (1981) Induction of hemoglobin accumulation in human K562 cells by hemin is reversible. Science 212: 459-461
    • (1981) Science , vol.212 , pp. 459-461
    • Dean, A.1    Erard, F.2    Schneider, A.P.3    Schechter, A.N.4
  • 16
    • 0027405813 scopus 로고
    • Regulation by heme of mitochondrial protein transport through a conserved amino acid motif
    • 16 Lathrop J. T. and Timko M. P. (1993) Regulation by heme of mitochondrial protein transport through a conserved amino acid motif. Science 259: 522-525
    • (1993) Science , vol.259 , pp. 522-525
    • Lathrop, J.T.1    Timko, M.P.2
  • 18
    • 0014429488 scopus 로고
    • The electronic structure of protoheme proteins. 3. Configuration of the heme and its ligands
    • 18 Peisach J., Blumberg W. E., Wittenberg B. A. and Wittenberg J. B. (1968) The electronic structure of protoheme proteins. 3. Configuration of the heme and its ligands. J. Biol. Chem. 243: 1871-1880
    • (1968) J. Biol. Chem. , vol.243 , pp. 1871-1880
    • Peisach, J.1    Blumberg, W.E.2    Wittenberg, B.A.3    Wittenberg, J.B.4
  • 19
    • 0002527001 scopus 로고
    • The spectra of ferric haems and haemoproteins
    • 19 Smith D. W. and Williams R. J. P. (1970) The spectra of ferric haems and haemoproteins. Structure Bonding 7: 1-45
    • (1970) Structure Bonding , vol.7 , pp. 1-45
    • Smith, D.W.1    Williams, R.J.P.2
  • 20
    • 0024979286 scopus 로고
    • Functional dissection and sequence of yeast HAP1 activator
    • 20 Pfeifer K., Kim K. S., Kogan S. and Guarente L. (1989) Functional dissection and sequence of yeast HAP1 activator. Cell 56: 291-301
    • (1989) Cell , vol.56 , pp. 291-301
    • Pfeifer, K.1    Kim, K.S.2    Kogan, S.3    Guarente, L.4
  • 21
    • 0024293409 scopus 로고
    • CYP1 (HAP1) regulator of oxygen-dependent gene expression in yeast. I. Overall organization of the protein sequence displays several novel structural domains
    • 21 Creusot F., Verdiere J., Gaisne M. and Slonimski P. P. (1988) CYP1 (HAP1) regulator of oxygen-dependent gene expression in yeast. I. Overall organization of the protein sequence displays several novel structural domains. J. Mol. Biol. 204: 263-276
    • (1988) J. Mol. Biol. , vol.204 , pp. 263-276
    • Creusot, F.1    Verdiere, J.2    Gaisne, M.3    Slonimski, P.P.4
  • 22
    • 0021473028 scopus 로고
    • Isolation and properties of 5-aminolevulinate synthase from the yeast Saccharomyces cerevisiae
    • 22 Volland C. and Felix F. (1984) Isolation and properties of 5-aminolevulinate synthase from the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 142: 551-557
    • (1984) Eur. J. Biochem. , vol.142 , pp. 551-557
    • Volland, C.1    Felix, F.2
  • 23
    • 0023657151 scopus 로고
    • Characterization of the yeast HEM2 gene and transcriptional regulation of COX5 and COR1 by heme
    • 23 Myers A. M., Crivellone M. D., Koerner T. J. and Tzagoloff A. (1987) Characterization of the yeast HEM2 gene and transcriptional regulation of COX5 and COR1 by heme. J. Biol. Chem. 262: 16822-16829
    • (1987) J. Biol. Chem. , vol.262 , pp. 16822-16829
    • Myers, A.M.1    Crivellone, M.D.2    Koerner, T.J.3    Tzagoloff, A.4
  • 24
    • 0026697908 scopus 로고
    • Structure and regulation of yeast HEM3, the gene for porphobilinogen deaminase
    • 24 Keng T., Richard C. and Larocque R. (1992) Structure and regulation of yeast HEM3, the gene for porphobilinogen deaminase. Mol. Gen. Genet. 234: 233-243
    • (1992) Mol. Gen. Genet. , vol.234 , pp. 233-243
    • Keng, T.1    Richard, C.2    Larocque, R.3
  • 25
    • 0028949282 scopus 로고
    • Isolation of the gene HEM4 encoding uroporphyrinogen III synthase in Saccharomyces cerevisiae
    • 25 Amillet J. M. and Labbe-Bois R. (1995) Isolation of the gene HEM4 encoding uroporphyrinogen III synthase in Saccharomyces cerevisiae. Yeast 11: 419-424
    • (1995) Yeast , vol.11 , pp. 419-424
    • Amillet, J.M.1    Labbe-Bois, R.2
  • 26
    • 0026578588 scopus 로고
    • Uroporphyrinogen decarboxylase in Saccharomyces cerevisiae. HEM12 gene sequence and evidence for two conserved glycines essential for enzymatic activity
    • 26 Garey J. R., Labbe-Bois R., Chelstowska A., Rytka J., Harrison L., Kushner J. et al. (1992) Uroporphyrinogen decarboxylase in Saccharomyces cerevisiae. HEM12 gene sequence and evidence for two conserved glycines essential for enzymatic activity. Eur. J. Biochem. 205: 1011-1016
    • (1992) Eur. J. Biochem. , vol.205 , pp. 1011-1016
    • Garey, J.R.1    Labbe-Bois, R.2    Chelstowska, A.3    Rytka, J.4    Harrison, L.5    Kushner, J.6
  • 27
    • 0023758444 scopus 로고
    • Isolation, sequence and regulation by oxygen of the yeast HEM13 gene coding for coproporphyrinogen oxidase
    • 27 Zagorec M., Buhler J. M., Treich I., Keng T., Guarente L. and Labbe-Bois R. (1988) Isolation, sequence and regulation by oxygen of the yeast HEM13 gene coding for coproporphyrinogen oxidase. J. Biol. Chem. 263; 9718-9724
    • (1988) J. Biol. Chem. , vol.263 , pp. 9718-9724
    • Zagorec, M.1    Buhler, J.M.2    Treich, I.3    Keng, T.4    Guarente, L.5    Labbe-Bois, R.6
  • 28
    • 0030012328 scopus 로고    scopus 로고
    • Cloning and characterization of the yeast HEM14 gene coding for protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides
    • 28 Camadro J. M. and Labbe P. (1996) Cloning and characterization of the yeast HEM14 gene coding for protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides. J. Biol. Chem. 271: 9120-9128
    • (1996) J. Biol. Chem. , vol.271 , pp. 9120-9128
    • Camadro, J.M.1    Labbe, P.2
  • 29
    • 0025267366 scopus 로고
    • The ferrochelatase from Saccharomyces cerevisiae. Sequence, disruption and expression of its structural gene HEM15
    • 29 Labbe-Bois R. (1990) The ferrochelatase from Saccharomyces cerevisiae. Sequence, disruption and expression of its structural gene HEM15. J. Biol. Chem. 265: 7278-7283
    • (1990) J. Biol. Chem. , vol.265 , pp. 7278-7283
    • Labbe-Bois, R.1
  • 30
    • 0029068817 scopus 로고
    • Isolation and characterization of extragenic mutations affecting the expression of the uroporphyrinogen decarboxylase gene (HEM12) in Sacharomyces cerevisiae
    • 30 Zoladek T., Chelstowska A., Labbe-Bois R. and Rytka J. (1995) Isolation and characterization of extragenic mutations affecting the expression of the uroporphyrinogen decarboxylase gene (HEM12) in Sacharomyces cerevisiae. Mol. Gen. Genet. 247: 471-481
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 471-481
    • Zoladek, T.1    Chelstowska, A.2    Labbe-Bois, R.3    Rytka, J.4
  • 31
    • 0026635664 scopus 로고
    • HAP1 and ROX1 form a regulatory pathway in the repression of HEM13 transcription in Saccharomyces cerevisiae
    • 31 Keng T. (1992) HAP1 and ROX1 form a regulatory pathway in the repression of HEM13 transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 12: 2616-2623
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2616-2623
    • Keng, T.1
  • 32
    • 0032052761 scopus 로고    scopus 로고
    • Oxygen sensing and the transcriptional regulation of oxygen-responsive genes in yeast
    • 32 Kwast K. E., Burke P. V. and Poyton R. O. (1998) Oxygen sensing and the transcriptional regulation of oxygen-responsive genes in yeast. J. Exp. Biol. 201: 1177-1195
    • (1998) J. Exp. Biol. , vol.201 , pp. 1177-1195
    • Kwast, K.E.1    Burke, P.V.2    Poyton, R.O.3
  • 33
    • 0021278372 scopus 로고
    • Distinctly regulated tandem upstream activation sites mediate catabolite repression of the CYC1 gene of S. cerevisiae
    • 33 Guarente L., Lalonde B., Gifford P. and Alani E. (1984) Distinctly regulated tandem upstream activation sites mediate catabolite repression of the CYC1 gene of S. cerevisiae. Cell 36: 503-511
    • (1984) Cell , vol.36 , pp. 503-511
    • Guarente, L.1    Lalonde, B.2    Gifford, P.3    Alani, E.4
  • 34
    • 0023768278 scopus 로고
    • ROX1 encodes a heme-induced repression factor regulating ANB1 and CYC7 of Saccharomyces cerevisiae
    • 34 Lowry C. V. and Zitomer R. S. (1988) ROX1 encodes a heme-induced repression factor regulating ANB1 and CYC7 of Saccharomyces cerevisiae. Mol. Cell. Biol. 8: 4651-4658
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4651-4658
    • Lowry, C.V.1    Zitomer, R.S.2
  • 35
    • 0023409211 scopus 로고
    • Organization of the regulatory region of the yeast CYC7 gene: Multiple factors are involved in regulation
    • 35 Prezant T., Pfeifer K. and Guarente L. (1987) Organization of the regulatory region of the yeast CYC7 gene: multiple factors are involved in regulation. Mol. Cell. Biol. 7: 3252-3259
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3252-3259
    • Prezant, T.1    Pfeifer, K.2    Guarente, L.3
  • 36
    • 0025999808 scopus 로고
    • Regulation of the yeast CYT1 gene encoding cytochrome c1 by HAP1 and HAP2/3/4
    • 36 Schneider J. C. and Guarente L. (1991) Regulation of the yeast CYT1 gene encoding cytochrome c1 by HAP1 and HAP2/3/4. Mol. Cell. Biol. 11: 4934-4942
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4934-4942
    • Schneider, J.C.1    Guarente, L.2
  • 37
    • 0024026479 scopus 로고
    • Co-ordinate control of synthesis of mitochondrial and non-mitochondrial hemoproteins: A binding site for the HAP1 (CYP1) protein in the UAS region of the yeast catalase T gene (CTT1)
    • 37 Winkler H., Adam G., Mattes E., Schanz M., Hartig A. and Ruis H. (1988) Co-ordinate control of synthesis of mitochondrial and non-mitochondrial hemoproteins: a binding site for the HAP1 (CYP1) protein in the UAS region of the yeast catalase T gene (CTT1). Embo J. 7: 1799-1804
    • (1988) Embo J. , vol.7 , pp. 1799-1804
    • Winkler, H.1    Adam, G.2    Mattes, E.3    Schanz, M.4    Hartig, A.5    Ruis, H.6
  • 38
    • 0025797255 scopus 로고
    • Complex transcriptional regulation of the Saccharomyces cerevisiae CYB2 gene encoding cytochrome b2: CYP1(HAP1) activator binds to the CYB2 upstream activation site UAS1-B2
    • 38 Lodi T. and Guiard B. (1991) Complex transcriptional regulation of the Saccharomyces cerevisiae CYB2 gene encoding cytochrome b2: CYP1(HAP1) activator binds to the CYB2 upstream activation site UAS1-B2. Mol. Cell. Biol. 11: 3762-3772
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3762-3772
    • Lodi, T.1    Guiard, B.2
  • 39
    • 0028818262 scopus 로고
    • Mutational analysis of Rox1, a DNA-bending repressor of hypoxic genes in Saccharomyces cerevisiae
    • 39 Deckert J., Rodriguez Torres A. M., Simon J. T. and Zitomer R. S. (1995) Mutational analysis of Rox1, a DNA-bending repressor of hypoxic genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 15: 6109-6117
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6109-6117
    • Deckert, J.1    Rodriguez Torres, A.M.2    Simon, J.T.3    Zitomer, R.S.4
  • 40
    • 0028898763 scopus 로고
    • Multiple elements and auto-repression regulate Rox1, a repressor of hypoxic genes in Saccharomyces cerevisiae
    • 40 Deckert J., Perini R., Balasubramanian B. and Zitomer R. S. (1995) Multiple elements and auto-repression regulate Rox1, a repressor of hypoxic genes in Saccharomyces cerevisiae. Genetics 139: 1149-1158
    • (1995) Genetics , vol.139 , pp. 1149-1158
    • Deckert, J.1    Perini, R.2    Balasubramanian, B.3    Zitomer, R.S.4
  • 41
    • 0032540362 scopus 로고    scopus 로고
    • Flavohemoglobin expression and function in Saccharomyces cerevisiae. No relationship with respiration and complex response to oxidative stress
    • 41 Buisson N. and Labbe-Bois R. (1998) Flavohemoglobin expression and function in Saccharomyces cerevisiae. No relationship with respiration and complex response to oxidative stress. J. Biol. Chem. 273: 9527-9533
    • (1998) J. Biol. Chem. , vol.273 , pp. 9527-9533
    • Buisson, N.1    Labbe-Bois, R.2
  • 42
    • 0029818837 scopus 로고    scopus 로고
    • Function and expression of flavohemoglobin in Saccharomyces cerevisiae. Evidence for a role in the oxidative stress response
    • 42 Zhao X. J., Raitt D., V Burke P., Clewell A. S., Kwast K. E. and Poyton R. O. (1996) Function and expression of flavohemoglobin in Saccharomyces cerevisiae. Evidence for a role in the oxidative stress response. J. Biol. Chem. 271: 25131-25138
    • (1996) J. Biol. Chem. , vol.271 , pp. 25131-25138
    • Zhao, X.J.1    Raitt, D.2    V Burke, P.3    Clewell, A.S.4    Kwast, K.E.5    Poyton, R.O.6
  • 43
    • 0020739930 scopus 로고
    • Heme regulates transcription of the CYC1 gene of S. cerevisiae via an upstream activation site
    • 43 Guarente L. and Mason T. (1983) Heme regulates transcription of the CYC1 gene of S. cerevisiae via an upstream activation site. Cell 32: 1279-1286
    • (1983) Cell , vol.32 , pp. 1279-1286
    • Guarente, L.1    Mason, T.2
  • 44
    • 0020393425 scopus 로고
    • Regulation of synthesis of catalases and iso-l-cytochrome c in Saccharomyces cerevisiae by glucose, oxygen and heme
    • 44 Hortner H., Ammerer G., Hartter E., Hamilton B., Rytka J., Bilinski T. et al. (1982) Regulation of synthesis of catalases and iso-l-cytochrome c in Saccharomyces cerevisiae by glucose, oxygen and heme. Eur. J. Biochem. 128: 179-184
    • (1982) Eur. J. Biochem. , vol.128 , pp. 179-184
    • Hortner, H.1    Ammerer, G.2    Hartter, E.3    Hamilton, B.4    Rytka, J.5    Bilinski, T.6
  • 45
    • 0025739041 scopus 로고
    • CYP1 (HAP1) is a determinant effector of alternative expression of heme- dependent transcribed genes in yeast
    • published erratum appears in Mol. Gen. Genet. 1991 Oct;229(2):324
    • 45 Verdiere J., Gaisne M. and Labbe B. R. (1991) CYP1 (HAP1) is a determinant effector of alternative expression of heme- dependent transcribed genes in yeast [corrected] [published erratum appears in Mol. Gen. Genet. 1991 Oct;229(2):324]. Mol. Gen. Genet. 228: 300-306
    • (1991) Mol. Gen. Genet. , vol.228 , pp. 300-306
    • Verdiere, J.1    Gaisne, M.2    Labbe, B.R.3
  • 46
    • 0028297158 scopus 로고
    • A novel allele of HAP1 causes uninducible expression of HEM13 in Saccharomyces cerevisiae
    • 46 Ushinsky S. C. and Keng T. (1994) A novel allele of HAP1 causes uninducible expression of HEM13 in Saccharomyces cerevisiae. Genetics 136: 819-831
    • (1994) Genetics , vol.136 , pp. 819-831
    • Ushinsky, S.C.1    Keng, T.2
  • 47
    • 0028821439 scopus 로고
    • Heme binds to a short sequence that serves a regulatory function in diverse proteins
    • 47 Zhang L. and Guarente L. (1995) Heme binds to a short sequence that serves a regulatory function in diverse proteins. Embo. J. 14: 313-320
    • (1995) Embo. J. , vol.14 , pp. 313-320
    • Zhang, L.1    Guarente, L.2
  • 48
    • 0027400951 scopus 로고
    • Evidence for an interaction between the CYP1(HAP1) activator and a cellular factor during heme-dependent transcriptional regulation in the yeast Saccharomyces cerevisiae
    • 48 Fytlovich S., Gervais M., Agrimonti C. and Guiard B. (1993) Evidence for an interaction between the CYP1(HAP1) activator and a cellular factor during heme-dependent transcriptional regulation in the yeast Saccharomyces cerevisiae. Embo. J. 12: 1209-1218
    • (1993) Embo. J. , vol.12 , pp. 1209-1218
    • Fytlovich, S.1    Gervais, M.2    Agrimonti, C.3    Guiard, B.4
  • 49
    • 0031009957 scopus 로고    scopus 로고
    • Heme regulates SOD2 transcription by activation and repression in Saccharomyces cerevisiae
    • 49 Pinkham J. L., Wang Z. and Alsina J. (1997) Heme regulates SOD2 transcription by activation and repression in Saccharomyces cerevisiae. Curr. Genet. 31: 281-291
    • (1997) Curr. Genet. , vol.31 , pp. 281-291
    • Pinkham, J.L.1    Wang, Z.2    Alsina, J.3
  • 50
    • 0028195088 scopus 로고
    • Functional analysis of the zinc cluster domain of the CYP1 (HAP1) complex regulator in heme-sufficient and heme-deficient yeast cells
    • 50 Defranoux N., Gaisne M. and Verdière J. (1994) Functional analysis of the zinc cluster domain of the CYP1 (HAP1) complex regulator in heme-sufficient and heme-deficient yeast cells. Mol. Gen. Genet. 242: 699-707
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 699-707
    • Defranoux, N.1    Gaisne, M.2    Verdière, J.3
  • 51
    • 0031887447 scopus 로고    scopus 로고
    • The transcriptional regulator Hap1p (Cyp1p) is essential for anaerobic or heme-deficient growth of Saccharomyces cerevisiae: Genetic and molecular characterization of an extragenic suppressor that encodes a WD repeat protein
    • 51 Chantrel Y., Gaisne M., Lions C. and Verdière J. (1998) The transcriptional regulator Hap1p (Cyp1p) is essential for anaerobic or heme-deficient growth of Saccharomyces cerevisiae: genetic and molecular characterization of an extragenic suppressor that encodes a WD repeat protein. Genetics 148: 559-569
    • (1998) Genetics , vol.148 , pp. 559-569
    • Chantrel, Y.1    Gaisne, M.2    Lions, C.3    Verdière, J.4
  • 52
    • 0028211739 scopus 로고
    • Evidence that TUP1/SSN6 has a positive effect on the activity of the yeast activator HAP1
    • 52 Zhang L. and Guarente L. (1994) Evidence that TUP1/SSN6 has a positive effect on the activity of the yeast activator HAP1. Genetics 136: 813-817
    • (1994) Genetics , vol.136 , pp. 813-817
    • Zhang, L.1    Guarente, L.2
  • 53
    • 0029811436 scopus 로고    scopus 로고
    • The C6 zinc cluster dictates asymmetric binding by HAP1
    • 53 Zhang L. and Guarente L. (1996) The C6 zinc cluster dictates asymmetric binding by HAP1. Embo. J. 15: 4676-4681
    • (1996) Embo. J. , vol.15 , pp. 4676-4681
    • Zhang, L.1    Guarente, L.2
  • 54
    • 0032899753 scopus 로고    scopus 로고
    • Structure of a HAP1/DNA complex reveals dramatically asymmetric DNA binding by a homodimeric protein
    • 54 King D. A., Zhang L., Guarente L. and Marmorstein R. (1999) Structure of a HAP1/DNA complex reveals dramatically asymmetric DNA binding by a homodimeric protein. Nature Struct. Biol. 6: 64-71
    • (1999) Nature Struct. Biol. , vol.6 , pp. 64-71
    • King, D.A.1    Zhang, L.2    Guarente, L.3    Marmorstein, R.4
  • 55
    • 0030747268 scopus 로고    scopus 로고
    • NMR analysis of CYP1(HAP1) DNA binding domain-CYC1 upstream activation sequence interactions: Recognition of a CGG trinucleotide and of an additional thymine 5 bp downstream by the zinc cluster and the N-terminal extremity of the protein
    • 55 Vuidepot A. L., Bontems F., Gervais M., Guiard B., Shechter E. and Lallemand J. Y. (1997) NMR analysis of CYP1(HAP1) DNA binding domain-CYC1 upstream activation sequence interactions: recognition of a CGG trinucleotide and of an additional thymine 5 bp downstream by the zinc cluster and the N-terminal extremity of the protein. Nucleic Acids Res. 25: 3042-3050
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3042-3050
    • Vuidepot, A.L.1    Bontems, F.2    Gervais, M.3    Guiard, B.4    Shechter, E.5    Lallemand, J.Y.6
  • 56
    • 0031054127 scopus 로고    scopus 로고
    • Some DNA targets of the yeast CYP1 transcriptional activator are functionally asymmetric evidence of two half-sites with different affinities
    • 56 Näit-Kaoudjt R., Williams R., Guiard B. and Gervais M. (1997) Some DNA targets of the yeast CYP1 transcriptional activator are functionally asymmetric evidence of two half-sites with different affinities. Eur. J. Biochem. 244: 301-309
    • (1997) Eur. J. Biochem. , vol.244 , pp. 301-309
    • Näit-Kaoudjt, R.1    Williams, R.2    Guiard, B.3    Gervais, M.4
  • 57
    • 0023493883 scopus 로고
    • A model fungal gene regulatory mechanism: The GAL genes of Saccharomyces cerevisiae
    • 57 Johnston M. (1987) A model fungal gene regulatory mechanism: the GAL genes of Saccharomyces cerevisiae. Microbiol Rev 51: 458-476
    • (1987) Microbiol Rev , vol.51 , pp. 458-476
    • Johnston, M.1
  • 58
    • 0029162876 scopus 로고
    • Solution structure of the Kluyveromyces lactis LAC9 Cd2 Cys6 DNA-binding domain
    • 58 Gardner K. H., Anderson S. F. and Coleman J. E. (1995) Solution structure of the Kluyveromyces lactis LAC9 Cd2 Cys6 DNA-binding domain. Nature Struct. Biol. 2: 898-905
    • (1995) Nature Struct. Biol. , vol.2 , pp. 898-905
    • Gardner, K.H.1    Anderson, S.F.2    Coleman, J.E.3
  • 59
    • 0026547747 scopus 로고
    • DNA recognition by GAL4: Structure of a protein-DNA complex
    • 59 Marmorstein R., Carey M., Ptashne M. and Harrison S. C. (1992) DNA recognition by GAL4: structure of a protein-DNA complex [see comments]. Nature 356: 408-414
    • (1992) Nature , vol.356 , pp. 408-414
    • Marmorstein, R.1    Carey, M.2    Ptashne, M.3    Harrison, S.C.4
  • 60
    • 0027993285 scopus 로고
    • Crystal structure of a PPR1-DNA complex: DNA recognition by proteins containing a Zn2Cys6 binuclear cluster
    • 60 Marmorstein R. and Harrison S. C. (1994) Crystal structure of a PPR1-DNA complex: DNA recognition by proteins containing a Zn2Cys6 binuclear cluster. Genes Dev. 8: 2504-2512
    • (1994) Genes Dev. , vol.8 , pp. 2504-2512
    • Marmorstein, R.1    Harrison, S.C.2
  • 61
    • 0026792997 scopus 로고
    • The UAS(-MAL) is a bidirectional promotor element required for the expression of both the MAL61 and MAL62 genes of the Saccharomyces MAL6 locus
    • 61 Levine J., Tanouye L. and Michels C. A. (1992) The UAS(-MAL) is a bidirectional promotor element required for the expression of both the MAL61 and MAL62 genes of the Saccharomyces MAL6 locus. Curr. Genet. 22: 181-189
    • (1992) Curr. Genet. , vol.22 , pp. 181-189
    • Levine, J.1    Tanouye, L.2    Michels, C.A.3
  • 62
    • 0027218382 scopus 로고
    • Determinants of binding-site specificity among yeast C6 zinc cluster proteins
    • 62 Reece R. J. and Ptashne M. (1993) Determinants of binding-site specificity among yeast C6 zinc cluster proteins. Science 261: 909-911
    • (1993) Science , vol.261 , pp. 909-911
    • Reece, R.J.1    Ptashne, M.2
  • 63
    • 0024367337 scopus 로고
    • The Saccharomyces cerevisiae PUT3 activator protein associates with proline-specific upstream activation sequences
    • 63 Siddiqui A. H. and Brandriss M. C. (1989) The Saccharomyces cerevisiae PUT3 activator protein associates with proline-specific upstream activation sequences. Mol. Cell. Biol. 9: 4706-4712
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4706-4712
    • Siddiqui, A.H.1    Brandriss, M.C.2
  • 64
    • 0029005029 scopus 로고
    • Purification and binding properties of the Ma163p activator of Saccharomyces cerevisiae
    • 64 Sirenko O. I., Ni B. and Needleman R. B. (1995) Purification and binding properties of the Ma163p activator of Saccharomyces cerevisiae. Curr. Genet. 27: 5509-5516
    • (1995) Curr. Genet. , vol.27 , pp. 5509-5516
    • Sirenko, O.I.1    Ni, B.2    Needleman, R.B.3
  • 65
    • 0030596420 scopus 로고    scopus 로고
    • 1H, 15N resonance assignment and three-dimensional structure of CYP1 (HAP1) DNA-binding domain
    • 65 Timmerman J., Vuidepot A. L., Bontems F., Lallemand J. Y., Gervais M., Shechter E. et al. (1996) 1H, 15N resonance assignment and three-dimensional structure of CYP1 (HAP1) DNA-binding domain. J. Mol. Biol. 259: 792-804
    • (1996) J. Mol. Biol. , vol.259 , pp. 792-804
    • Timmerman, J.1    Vuidepot, A.L.2    Bontems, F.3    Lallemand, J.Y.4    Gervais, M.5    Shechter, E.6
  • 66
    • 0027536095 scopus 로고
    • Antibody-promoted dimerization bypasses the regulation of DNA binding by the heme domain of the yeast transcriptional activator HAP1
    • 66 Zhang L., Bermingham M. O., Turcotte B. and Guarente L. (1993) Antibody-promoted dimerization bypasses the regulation of DNA binding by the heme domain of the yeast transcriptional activator HAP1. Proc. Natl. Acad. Sci. USA 90: 2851-2855
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2851-2855
    • Zhang, L.1    Bermingham, M.O.2    Turcotte, B.3    Guarente, L.4
  • 67
    • 0028071873 scopus 로고
    • The yeast activator HAP1 a GAL4 family member binds DNA in a directly repeated orientation
    • 67 Zhang L. and Guarente L. (1994) The yeast activator HAP1 a GAL4 family member binds DNA in a directly repeated orientation. Genes Dev. 8: 2110-2119
    • (1994) Genes Dev. , vol.8 , pp. 2110-2119
    • Zhang, L.1    Guarente, L.2
  • 68
    • 0028302793 scopus 로고
    • HAP1 is nuclear but is bound to a cellular factor in the absence of heme
    • 68 Zhang L. and Guarente L. (1994) HAP1 is nuclear but is bound to a cellular factor in the absence of heme. J. Biol. Chem. 269: 14643-14647
    • (1994) J. Biol. Chem. , vol.269 , pp. 14643-14647
    • Zhang, L.1    Guarente, L.2
  • 69
    • 0031806619 scopus 로고    scopus 로고
    • Molecular mechanism governing heme signaling in yeast: A higher-order complex mediates heme regulation of the transcriptional activator HAP1
    • 69 Zhang L., Hach A. and Wang C. (1998) Molecular mechanism governing heme signaling in yeast: a higher-order complex mediates heme regulation of the transcriptional activator HAP1. Mol. Cell. Biol. 18: 3819-3828
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3819-3828
    • Zhang, L.1    Hach, A.2    Wang, C.3
  • 70
    • 0029047434 scopus 로고
    • Multiple domains mediate heme control of the yeast activator HAP1
    • 70 Haldi M. L. and Guarente L. (1995) Multiple domains mediate heme control of the yeast activator HAP1. Mol. Gen. Genet. 248: 229-235
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 229-235
    • Haldi, M.L.1    Guarente, L.2
  • 72
    • 0029026540 scopus 로고
    • Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways
    • 72 Kimura Y., Yahara I. and Lindquist S. (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways [see comments]. Science 268: 1362-1365
    • (1995) Science , vol.268 , pp. 1362-1365
    • Kimura, Y.1    Yahara, I.2    Lindquist, S.3
  • 73
    • 15144346211 scopus 로고    scopus 로고
    • Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70
    • 73 Maheswaran S., Englert C., Zheng G., Lee S., Wong J., Harkin D. et al. (1998) Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70. Genes Dev. 12: 1108-1120
    • (1998) Genes Dev. , vol.12 , pp. 1108-1120
    • Maheswaran, S.1    Englert, C.2    Zheng, G.3    Lee, S.4    Wong, J.5    Harkin, D.6
  • 74
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • 74 Shi Y., Mosser D. and Morimoto R. (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12: 654-666
    • (1998) Genes Dev. , vol.12 , pp. 654-666
    • Shi, Y.1    Mosser, D.2    Morimoto, R.3
  • 75
    • 0031911786 scopus 로고    scopus 로고
    • Regulation of transcription factor Pdr1p function by an Hsp70 protein in Saccharomyces cerevisiae
    • 75 Hallstrom T. C., Katzmann D. J., Torres R. J., Sharp W. J. and Moye-Rowley W. S. (1998) Regulation of transcription factor Pdr1p function by an Hsp70 protein in Saccharomyces cerevisiae. Mol. Cell. Biol. 18: 1147-1155
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1147-1155
    • Hallstrom, T.C.1    Katzmann, D.J.2    Torres, R.J.3    Sharp, W.J.4    Moye-Rowley, W.S.5
  • 76
    • 0033049803 scopus 로고    scopus 로고
    • A new class of repression modules is critical for heme regulation of the yeast transcriptional activator Hap1
    • 76 Hach A., Hon T. and Zhang L. (1999) A new class of repression modules is critical for heme regulation of the yeast transcriptional activator Hap1. Mol.Cell. Biol. 19: 4324-4333
    • (1999) Mol.cell. Biol. , vol.19 , pp. 4324-4333
    • Hach, A.1    Hon, T.2    Zhang, L.3
  • 77
    • 0033529548 scopus 로고    scopus 로고
    • The yeast heme-responsive transcriptional activator Hap1 is a preexisting dimer in the absence of heme
    • 76a Hon T., Hach A., Tamalis D., Zhu Y. and Zhang L. (1999) The yeast heme-responsive transcriptional activator Hap1 is a preexisting dimer in the absence of heme. J. Biol. Chem. 274: 22770-22774
    • (1999) J. Biol. Chem. , vol.274 , pp. 22770-22774
    • Hon, T.1    Hach, A.2    Tamalis, D.3    Zhu, Y.4    Zhang, L.5
  • 78
    • 0028858102 scopus 로고
    • Hsp90 mutants disrupt glucocortocoid receptor ligand binding and destabilize aporeceptor complexes
    • 77 Bohen S. P. (1995) Hsp90 mutants disrupt glucocortocoid receptor ligand binding and destabilize aporeceptor complexes. J. Biol. Chem. 270: 29433-29438
    • (1995) J. Biol. Chem. , vol.270 , pp. 29433-29438
    • Bohen, S.P.1
  • 79
    • 0029985050 scopus 로고    scopus 로고
    • Hsp90 regulates androgen receptor hormone binding affinity in vivo
    • 78 Fang Y., Fliss A. E., Robins D. M. and Caplan A. J. (1996) Hsp90 regulates androgen receptor hormone binding affinity in vivo. J. Biol. Chem. 271: 28697-28702
    • (1996) J. Biol. Chem. , vol.271 , pp. 28697-28702
    • Fang, Y.1    Fliss, A.E.2    Robins, D.M.3    Caplan, A.J.4
  • 80
    • 0025745326 scopus 로고
    • Characterization of YDJ1: A yeast homologue of the bacterial dnaJ protein
    • 79 Caplan A. J. and Douglas M. G. (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J. Cell. Biol. 114: 609-621
    • (1991) J. Cell. Biol. , vol.114 , pp. 609-621
    • Caplan, A.J.1    Douglas, M.G.2
  • 81
    • 0028898217 scopus 로고
    • Hormone-dependent transactivation by the human androgen receptor is regulated by a dnaj protein
    • 80 Caplan A. J., Langley E., Wilson E. M. and Vidal J. (1995) Hormone-dependent transactivation by the human androgen receptor is regulated by a dnaJ protein. J. Biol. Chem. 270: 5251-5257
    • (1995) J. Biol. Chem. , vol.270 , pp. 5251-5257
    • Caplan, A.J.1    Langley, E.2    Wilson, E.M.3    Vidal, J.4
  • 82
    • 0026739395 scopus 로고
    • Regulation of Hsp70 function by a eukaryotic DnaJ homolog
    • 81 Cyr D. M., Lu X. and Douglas M. G. (1992) Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J. Biol. Chem. 267: 20927-20931
    • (1992) J. Biol. Chem. , vol.267 , pp. 20927-20931
    • Cyr, D.M.1    Lu, X.2    Douglas, M.G.3
  • 83
    • 0025220996 scopus 로고
    • Characterization of TUP1, a mediator of glucose repression in Saccharomyces cerevisiae
    • 82 Williams F. E. and Trumbly R. J. (1990) Characterization of TUP1, a mediator of glucose repression in Saccharomyces cerevisiae. Mol. Cell. Biol. 10: 6500-6511
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6500-6511
    • Williams, F.E.1    Trumbly, R.J.2
  • 84
    • 0024256134 scopus 로고
    • Cloning and characterization of the CYC8 gene mediating glucose repression in yeast
    • 83 Trumbly R. J. (1988) Cloning and characterization of the CYC8 gene mediating glucose repression in yeast. Gene 73: 97-111
    • (1988) Gene , vol.73 , pp. 97-111
    • Trumbly, R.J.1
  • 85
    • 0029965550 scopus 로고    scopus 로고
    • The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and four Tup1 subunits
    • 84 Varanasi U. S., Klis M., Mikesell P. B. and Trumbly R. J. (1996) The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and four Tup1 subunits. Mol. Cell. Biol. 16: 6707-6714
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6707-6714
    • Varanasi, U.S.1    Klis, M.2    Mikesell, P.B.3    Trumbly, R.J.4
  • 86
    • 0025122590 scopus 로고
    • The N-terminal TPR region is the functional domain of SSN6, a nuclear phosphoprotein of Saccharomyces cerevisiae
    • published erratum appears in Mol. Cell. Biol. 1992 Jun;12(6):2909
    • 85 Schultz J., Marshall-Carlson L. and Carlson M. (1990) The N-terminal TPR region is the functional domain of SSN6, a nuclear phosphoprotein of Saccharomyces cerevisiae [published erratum appears in Mol. Cell. Biol. 1992 Jun;12(6):2909]. Mol. Cell. Biol. 10: 4744-4756
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4744-4756
    • Schultz, J.1    Marshall-Carlson, L.2    Carlson, M.3
  • 87
    • 0023424198 scopus 로고
    • Molecular analysis of SSN6, a gene functionally related to the SNF1 protein kinase of Saccharomyces cerevisiae
    • 86 Schultz J. and Carlson M. (1987) Molecular analysis of SSN6, a gene functionally related to the SNF1 protein kinase of Saccharomyces cerevisiae. Mol. Cell. Biol. 7: 3637-3645
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3637-3645
    • Schultz, J.1    Carlson, M.2
  • 88
    • 0026571899 scopus 로고
    • Ssn6-Tup1 is a general repressor of transcription in yeast
    • 87 Keleher C. A., Redd M. J., Schultz J., Carlson M. and Johnson A. D. (1992) Ssn6-Tup1 is a general repressor of transcription in yeast. Cell 68: 709-719
    • (1992) Cell , vol.68 , pp. 709-719
    • Keleher, C.A.1    Redd, M.J.2    Schultz, J.3    Carlson, M.4    Johnson, A.D.5
  • 89
    • 0025015378 scopus 로고
    • The HAP2 subunit of yeast CCAAT transcriptional activator contains adjacent domains for subunit association and DNA recognition: Model for the HAP2/3/4 complex
    • 88 Olesen J. T. and Guarente L. (1990) The HAP2 subunit of yeast CCAAT transcriptional activator contains adjacent domains for subunit association and DNA recognition: model for the HAP2/3/4 complex. Genes Dev. 4: 1714-1729
    • (1990) Genes Dev. , vol.4 , pp. 1714-1729
    • Olesen, J.T.1    Guarente, L.2
  • 90
    • 0024713582 scopus 로고
    • Identification and characterization of HAP4: A third component of the CCAAT-bound HAP2/HAP3 heteromer
    • 89 Forsburg S. L. and Guarente L. (1989) Identification and characterization of HAP4: a third component of the CCAAT-bound HAP2/HAP3 heteromer. Genes Dev. 3: 1166-1178
    • (1989) Genes Dev. , vol.3 , pp. 1166-1178
    • Forsburg, S.L.1    Guarente, L.2
  • 91
    • 0028795797 scopus 로고
    • Cloning of yeast HAP5: A novel subunit of a heterotrimeric complex required for CCAAT binding
    • 90 McNabb D. S., Xing Y. and Guarente L. (1995) Cloning of yeast HAP5: a novel subunit of a heterotrimeric complex required for CCAAT binding. Genes Dev. 9: 47-58
    • (1995) Genes Dev. , vol.9 , pp. 47-58
    • McNabb, D.S.1    Xing, Y.2    Guarente, L.3
  • 92
    • 0032030308 scopus 로고    scopus 로고
    • A survey of 178 NF-Y binding CCAAT boxes
    • 91 Mantovani R. (1998) A survey of 178 NF-Y binding CCAAT boxes. Nucleic Acids Res. 26: 1135-1143
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1135-1143
    • Mantovani, R.1
  • 93
    • 0031017966 scopus 로고    scopus 로고
    • Transcriptional regulation of the ferritin heavy-chain gene: The activity of the CCAAT binding factor NF-Y is modulated in heme-treated friend leukemia cells and during monocyte-to-macrophage differentiation
    • 92 Marziali G., Perrotti E., Hari R., Testa U., Coccia E. M. and Ruttistini A. (1997) Transcriptional regulation of the ferritin heavy-chain gene: the activity of the CCAAT binding factor NF-Y is modulated in heme-treated Friend leukemia cells and during monocyte-to-macrophage differentiation. Mol. Cell. Biol. 17: 1387-1395
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1387-1395
    • Marziali, G.1    Perrotti, E.2    Hari, R.3    Testa, U.4    Coccia, E.M.5    Ruttistini, A.6
  • 94
    • 0029665751 scopus 로고    scopus 로고
    • Gln3p is capable of binding to UAS(-NTR) elements and activating transcription in Saccharomyces cerevisiae
    • 93 Cunningham T, S., Svetlov V. V., Rai R., Smart W. and Cooper T. G. (1996) Gln3p is capable of binding to UAS(-NTR) elements and activating transcription in Saccharomyces cerevisiae. J. Bacteriol. 178: 3470-3479
    • (1996) J. Bacteriol. , vol.178 , pp. 3470-3479
    • Cunningham, T.S.1    Svetlov, V.V.2    Rai, R.3    Smart, W.4    Cooper, T.G.5
  • 95
    • 0029070939 scopus 로고
    • Recognition of nitrogen-responsive upstream activation sequences of Saccharomyces cerevisiae by the product of the GLN3 gene
    • 94 Blinder D. and Magasanik B. (1995) Recognition of nitrogen-responsive upstream activation sequences of Saccharomyces cerevisiae by the product of the GLN3 gene. J. Bacteriol. 177: 4190-4193
    • (1995) J. Bacteriol. , vol.177 , pp. 4190-4193
    • Blinder, D.1    Magasanik, B.2
  • 96
    • 0021706678 scopus 로고
    • Regulation of glutamine-repressible gene products by the GLN3 function in Saccharomyces cerevisiae
    • 95 Mitchell A. P. and Magasanik B. (1984) Regulation of glutamine-repressible gene products by the GLN3 function in Saccharomyces cerevisiae. Mol. Cell. Biol. 4: 2758-2766
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2758-2766
    • Mitchell, A.P.1    Magasanik, B.2
  • 97
    • 0030010438 scopus 로고    scopus 로고
    • The CCAAT box-binding factor stimulates ammonium assimilation in Saccharomyces cerevisiae, defining a new cross-pathway regulation between nitrogen and carbon metabolisms
    • 96 Dang V. D., Bohn C., Bolotin-Fukuhara M. and Daignan-Fornier B. (1996) The CCAAT box-binding factor stimulates ammonium assimilation in Saccharomyces cerevisiae, defining a new cross-pathway regulation between nitrogen and carbon metabolisms. J. Bacteriol. 178: 1842-1849
    • (1996) J. Bacteriol. , vol.178 , pp. 1842-1849
    • Dang, V.D.1    Bohn, C.2    Bolotin-Fukuhara, M.3    Daignan-Fornier, B.4
  • 98
    • 0028876606 scopus 로고
    • Transcriptional and posttranslational regulation of the general amino acid permease of Saccharomyces cerevisiae
    • 97 Stanbrough M. and Magasanik B. (1995) Transcriptional and posttranslational regulation of the general amino acid permease of Saccharomyces cerevisiae. J. Bacteriol. 177: 94-102
    • (1995) J. Bacteriol. , vol.177 , pp. 94-102
    • Stanbrough, M.1    Magasanik, B.2
  • 99
    • 0027523893 scopus 로고
    • Regulatory circuit for responses of nitrogen catabolic gene expression to the GLN3 and DAL80 proteins and nitrogen catabolite repression in Saccharomyces cerevisiae
    • 98 Daugherty J. R., Rai R., El Berry H. M. and Cooper T. G. (1993) Regulatory circuit for responses of nitrogen catabolic gene expression to the GLN3 and DAL80 proteins and nitrogen catabolite repression in Saccharomyces cerevisiae. J. Bacteriol. 175: 64-73
    • (1993) J. Bacteriol. , vol.175 , pp. 64-73
    • Daugherty, J.R.1    Rai, R.2    El Berry, H.M.3    Cooper, T.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.