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Volumn 6, Issue 4, 2007, Pages 734-743

Basic helix-loop-helix transcription factor heterocomplex of Yas1p and Yas2p regulates cytochrome P450 expression in response to alkanes in the yeast Yarrowia lipolytica

Author keywords

[No Author keywords available]

Indexed keywords

ALKANE; BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; CYTOCHROME P450; FUNGAL DNA; FUNGAL PROTEIN; INOSITOL; MUTANT PROTEIN;

EID: 34247846159     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00412-06     Document Type: Article
Times cited : (45)

References (52)
  • 1
    • 0028363566 scopus 로고
    • INO2 and INO4 gene products, positive regulators of phospholipid biosynthesis in Saccharomyces cerevisiae form a complex that binds to the INO1 promoter
    • Ambroziak, J., and S. A. Henry. 1994. INO2 and INO4 gene products, positive regulators of phospholipid biosynthesis in Saccharomyces cerevisiae form a complex that binds to the INO1 promoter. J. Biol. Chem. 269:15344-15349.
    • (1994) J. Biol. Chem , vol.269 , pp. 15344-15349
    • Ambroziak, J.1    Henry, S.A.2
  • 2
    • 0031008399 scopus 로고    scopus 로고
    • A natural classification of the basic helix-loop-helix class of transcription factors
    • Atchley, W. R., and W. M. Fitch. 1997. A natural classification of the basic helix-loop-helix class of transcription factors. Proc. Natl. Acad. Sci. USA 94:5172-5176.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5172-5176
    • Atchley, W.R.1    Fitch, W.M.2
  • 3
    • 0028851909 scopus 로고
    • Functional characterization of an inositol-sensitive upstream activation sequence in yeast. A cis-regulatory element responsible for inositol-choline mediated regulation of phospholipid biosynthesis
    • Bachhawat, N., Q. Ouyang, and S. A. Henry. 1995. Functional characterization of an inositol-sensitive upstream activation sequence in yeast. A cis-regulatory element responsible for inositol-choline mediated regulation of phospholipid biosynthesis. J. Biol. Chem. 270:25087-25095.
    • (1995) J. Biol. Chem , vol.270 , pp. 25087-25095
    • Bachhawat, N.1    Ouyang, Q.2    Henry, S.A.3
  • 4
    • 0030925208 scopus 로고    scopus 로고
    • Physiology and genetics of the dimorphic fungus Yarrowia lipolytica
    • Barth, G., and C. Gaillardin. 1997. Physiology and genetics of the dimorphic fungus Yarrowia lipolytica. FEMS Microbiol Rev. 19:214-237.
    • (1997) FEMS Microbiol Rev , vol.19 , pp. 214-237
    • Barth, G.1    Gaillardin, C.2
  • 6
    • 0014939620 scopus 로고
    • The enzymatic hydroxylation of n-octane by Corynebacterium sp. strain 7E1C
    • Cardini, G., and P. Jurtshuk. 1970. The enzymatic hydroxylation of n-octane by Corynebacterium sp. strain 7E1C. J. Biol. Chem. 245:2789-2796.
    • (1970) J. Biol. Chem , vol.245 , pp. 2789-2796
    • Cardini, G.1    Jurtshuk, P.2
  • 8
    • 0034331073 scopus 로고    scopus 로고
    • Finding nuclear localization signals
    • Cokol, M., R. Nair, and B. Rost. 2000. Finding nuclear localization signals. EMBO Rep. 1:411-415.
    • (2000) EMBO Rep , vol.1 , pp. 411-415
    • Cokol, M.1    Nair, R.2    Rost, B.3
  • 9
    • 3042720475 scopus 로고    scopus 로고
    • Dujon, B, D. Sherman, G. Fischer, P. Durrens, S. Casaregola, I. Lafontaine, J. De Montigny, C. Marek, C. Neuveglise, E. Talla, N. Goffard, L. Frangeul, M. Aigle, V. Anthouard, A. Babour, V. Barbe, S. Barnay, S. Blanchin, J. M. Beckerich, E. Beyne, C. Bleykasten, A. Boisrame, J. Boyer, L. Cattolico, P. Confanioleri, A. De Daruvar, L. Despons, E. Fabre, C. Fairhead, H. Ferry-Dumazet, A. Groppi, F. Hantraye, C. Hennequin, N. Jauniaux, P. Joyet, R. Kachouri, A. Kerrest, K. Koszul, M. Lemaire, I. Lesur, L. Ma, H. Muller, J. M. Nicaud, M. Nikolski, S. Oztas, O. Ozier-Kalogeropoulos, S. Pellenz, S. Potier, G. F. Richard, M. L. Straub, A. Suleau, D. Swennen, F. Tekaia, M. Wesolowski-Louvel, K. Westhof, B. Wirth, M. Zenion-Meyer, I. Zivanovic, M. Bolotin-Fukuhara, A. Thierry, C. Bouchier, B. Caudron, C. Scarpelli, C. Gaillardin, J. Weissenbach, P. Wineker, and J. L. Souciet. 2004. Genome evolution in yeasts. Nature 430:35-44
    • Dujon, B., D. Sherman, G. Fischer, P. Durrens, S. Casaregola, I. Lafontaine, J. De Montigny, C. Marek, C. Neuveglise, E. Talla, N. Goffard, L. Frangeul, M. Aigle, V. Anthouard, A. Babour, V. Barbe, S. Barnay, S. Blanchin, J. M. Beckerich, E. Beyne, C. Bleykasten, A. Boisrame, J. Boyer, L. Cattolico, P. Confanioleri, A. De Daruvar, L. Despons, E. Fabre, C. Fairhead, H. Ferry-Dumazet, A. Groppi, F. Hantraye, C. Hennequin, N. Jauniaux, P. Joyet, R. Kachouri, A. Kerrest, K. Koszul, M. Lemaire, I. Lesur, L. Ma, H. Muller, J. M. Nicaud, M. Nikolski, S. Oztas, O. Ozier-Kalogeropoulos, S. Pellenz, S. Potier, G. F. Richard, M. L. Straub, A. Suleau, D. Swennen, F. Tekaia, M. Wesolowski-Louvel, K. Westhof, B. Wirth, M. Zenion-Meyer, I. Zivanovic, M. Bolotin-Fukuhara, A. Thierry, C. Bouchier, B. Caudron, C. Scarpelli, C. Gaillardin, J. Weissenbach, P. Wineker, and J. L. Souciet. 2004. Genome evolution in yeasts. Nature 430:35-44.
  • 10
    • 0034110941 scopus 로고    scopus 로고
    • Conservation of glutamine-rich transactivation function between yeast and humans
    • Escher, D., M. Bodmer-Glavas, A. Barberis, and W. Schaffner. 2000. Conservation of glutamine-rich transactivation function between yeast and humans. Mol. Cell. Biol. 20:2774-2782.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 2774-2782
    • Escher, D.1    Bodmer-Glavas, M.2    Barberis, A.3    Schaffner, W.4
  • 11
    • 0027910469 scopus 로고
    • Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
    • Ferre-D'Amare, A. R., G. C. Prendergast, E. B. Ziff, and S. K. Burley. 1993. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 363:38-45.
    • (1993) Nature , vol.363 , pp. 38-45
    • Ferre-D'Amare, A.R.1    Prendergast, G.C.2    Ziff, E.B.3    Burley, S.K.4
  • 12
  • 14
    • 23444458415 scopus 로고
    • Transcriptional activation modulated by homopolymeric glutamine and proline stretches
    • Gerber, H. P., K. Seipel, O. Georgiev, M. Hofferer, M. Hug, S. Rosconi, and W. Schaffner. 1994. Transcriptional activation modulated by homopolymeric glutamine and proline stretches. Science 263:808-811.
    • (1994) Science , vol.263 , pp. 808-811
    • Gerber, H.P.1    Seipel, K.2    Georgiev, O.3    Hofferer, M.4    Hug, M.5    Rosconi, S.6    Schaffner, W.7
  • 15
    • 0029963923 scopus 로고    scopus 로고
    • Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae
    • Greenberg, M. L., and J. M. Lopes. 1996. Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae. Microbiol. Rev. 60:1-20.
    • (1996) Microbiol. Rev , vol.60 , pp. 1-20
    • Greenberg, M.L.1    Lopes, J.M.2
  • 16
    • 0025249935 scopus 로고
    • The Saccharomyces cerevisiae INO4 gene encodes a small, highly basic protein required for derepression of phospholipid biosynthetic enzymes
    • Hoshizaki, D. K., J. E. Hill, and S. A. Henry. 1990. The Saccharomyces cerevisiae INO4 gene encodes a small, highly basic protein required for derepression of phospholipid biosynthetic enzymes. J. Biol. Chem. 265:4736-4745.
    • (1990) J. Biol. Chem , vol.265 , pp. 4736-4745
    • Hoshizaki, D.K.1    Hill, J.E.2    Henry, S.A.3
  • 17
    • 0032444679 scopus 로고    scopus 로고
    • Cloning and characterization of an n-alkane-inducible cytochrome P450 gene essential for n-decane assimilation by Yarrowia lipolytica
    • Iida, T., A. Ohta, and M. Takagi. 1998. Cloning and characterization of an n-alkane-inducible cytochrome P450 gene essential for n-decane assimilation by Yarrowia lipolytica. Yeast 14:1387-1397.
    • (1998) Yeast , vol.14 , pp. 1387-1397
    • Iida, T.1    Ohta, A.2    Takagi, M.3
  • 18
    • 0034666118 scopus 로고    scopus 로고
    • The cytochrome P450ALK multigene family of an n-alkane-assimilating yeast. Yarrowia lipolytica: Cloning and characterisation of genes coding for new CYP52 family members
    • Iida, T., T. Sumita, A. Ohta, and M. Takagi. 2000. The cytochrome P450ALK multigene family of an n-alkane-assimilating yeast. Yarrowia lipolytica: cloning and characterisation of genes coding for new CYP52 family members. Yeast 16:1077-1087.
    • (2000) Yeast , vol.16 , pp. 1077-1087
    • Iida, T.1    Sumita, T.2    Ohta, A.3    Takagi, M.4
  • 20
    • 13844276160 scopus 로고    scopus 로고
    • n-Alkane and clofibrate, a peroxisome proliferator, activate transcription of ALK2 gene encoding cytochrome P450alk2 through distinct cis-acting, promoter elements in Candida maltosa
    • Kogure, T., M. Takagi, and A. Ohta. 2005. n-Alkane and clofibrate, a peroxisome proliferator, activate transcription of ALK2 gene encoding cytochrome P450alk2 through distinct cis-acting, promoter elements in Candida maltosa. Biochem. Biophys. Res. Commun. 329:78-86.
    • (2005) Biochem. Biophys. Res. Commun , vol.329 , pp. 78-86
    • Kogure, T.1    Takagi, M.2    Ohta, A.3
  • 21
    • 0035834750 scopus 로고    scopus 로고
    • The Q-rich subdomain of the human Ab receptor transactivation domain is required for dioxin-mediated transcriptional activity
    • Kumar, M. B., P. Ramadoss, R. K. Reen, J. P. Vanden Heuvel, and G. H. Perdew. 2001. The Q-rich subdomain of the human Ab receptor transactivation domain is required for dioxin-mediated transcriptional activity. J. Biol. Chem. 276:42302-42310.
    • (2001) J. Biol. Chem , vol.276 , pp. 42302-42310
    • Kumar, M.B.1    Ramadoss, P.2    Reen, R.K.3    Vanden Heuvel, J.P.4    Perdew, G.H.5
  • 22
    • 0015211115 scopus 로고
    • Fatty acid and hydrocarbon hydroxylation in yeast: Role of cytochrome P-450 in Candida tropicalis
    • Lebeault, J. M., K. T. Lode, and M. J. Coon. 1971. Fatty acid and hydrocarbon hydroxylation in yeast: role of cytochrome P-450 in Candida tropicalis. Biochem. Biophys. Res. Commun. 42:413-419.
    • (1971) Biochem. Biophys. Res. Commun , vol.42 , pp. 413-419
    • Lebeault, J.M.1    Lode, K.T.2    Coon, M.J.3
  • 24
  • 25
    • 0028215362 scopus 로고
    • Crystal structure of MyoD bHLH domain-DNA complex: Perspectives on DNA recognition and implications for transcriptional activation
    • Ma, P. C., M. A. Rould, H. Weintraub, and C. O. Palm. 1994. Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation. Cell 77:451-459.
    • (1994) Cell , vol.77 , pp. 451-459
    • Ma, P.C.1    Rould, M.A.2    Weintraub, H.3    Palm, C.O.4
  • 26
    • 0033980393 scopus 로고    scopus 로고
    • Helix-loop-helix proteins: Regulators of transcription in eucaryotic organisms
    • Massari, M. E., and C. Murre. 2000. Helix-loop-helix proteins: regulators of transcription in eucaryotic organisms. Mol. Cell. Biol. 20:429-440.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 429-440
    • Massari, M.E.1    Murre, C.2
  • 27
    • 0024396320 scopus 로고
    • Transcriptional regulation in mammalian cells by sequenee-specific DNA binding proteins
    • Mitchell, P. J., and R. Tjian. 1989. Transcriptional regulation in mammalian cells by sequenee-specific DNA binding proteins. Science 245:371-378.
    • (1989) Science , vol.245 , pp. 371-378
    • Mitchell, P.J.1    Tjian, R.2
  • 30
    • 0027126924 scopus 로고
    • The INO2 gene of Saccharomyces cerevisiae encodes a helix-loop-helix protein that is required for activation of phospholipid synthesis
    • Nikoloff, D. M., P. McGraw, and S. A. Henry. 1992. The INO2 gene of Saccharomyces cerevisiae encodes a helix-loop-helix protein that is required for activation of phospholipid synthesis. Nucleic Acids Res. 20:3253.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3253
    • Nikoloff, D.M.1    McGraw, P.2    Henry, S.A.3
  • 31
    • 0028987581 scopus 로고
    • CYP52 (cytochrome P450alk) multigene family in Candida maltosa: Identification and characterization of eight members
    • Ohkuma, M., S. Muraoka, T. Tanimoto, M. Fujii, A. Ohta, and M. Takagi. 1995. CYP52 (cytochrome P450alk) multigene family in Candida maltosa: identification and characterization of eight members. DNA Cell Biol. 14: 163-173.
    • (1995) DNA Cell Biol , vol.14 , pp. 163-173
    • Ohkuma, M.1    Muraoka, S.2    Tanimoto, T.3    Fujii, M.4    Ohta, A.5    Takagi, M.6
  • 32
    • 0026161236 scopus 로고
    • CYP52 (cytochrome p450alk) multigene family in Candida maltosa: Molecular cloning and nucleotide sequence of the two tandemly arranged genes
    • Ohkuma, M., T. Tanimoto, K. Yano, and M. Takani. 1991. CYP52 (cytochrome p450alk) multigene family in Candida maltosa: molecular cloning and nucleotide sequence of the two tandemly arranged genes. DNA Cell Biol. 10:271-282.
    • (1991) DNA Cell Biol , vol.10 , pp. 271-282
    • Ohkuma, M.1    Tanimoto, T.2    Yano, K.3    Takani, M.4
  • 33
    • 0030774035 scopus 로고    scopus 로고
    • Three classes of mammalian transcription activation domain stimulate transcription in Schizosaccharomyces pombe
    • Remacle, J. E., G. Albrecht, R. Brys, G. H. Braus, and D. Huylebroeck. 1997. Three classes of mammalian transcription activation domain stimulate transcription in Schizosaccharomyces pombe. EMBO J. 16:5722-5729.
    • (1997) EMBO J , vol.16 , pp. 5722-5729
    • Remacle, J.E.1    Albrecht, G.2    Brys, R.3    Braus, G.H.4    Huylebroeck, D.5
  • 35
    • 0034164664 scopus 로고    scopus 로고
    • Robinson, K. A., and J. M. Lopes. 2000. SURVEY AND SUMMARY: Saccharomyces cerevisiae basic helix-loop-helix proteins regulate diverse biological processes. Nucleic Acids Res. 28:1499-1505.
    • Robinson, K. A., and J. M. Lopes. 2000. SURVEY AND SUMMARY: Saccharomyces cerevisiae basic helix-loop-helix proteins regulate diverse biological processes. Nucleic Acids Res. 28:1499-1505.
  • 36
    • 0029917720 scopus 로고    scopus 로고
    • Myc oncogenes: The enigmatic family
    • Ryan, K. M., and G. D. Birnie. 1996. Myc oncogenes: the enigmatic family. Biochem. J. 314:713-721.
    • (1996) Biochem. J , vol.314 , pp. 713-721
    • Ryan, K.M.1    Birnie, G.D.2
  • 37
    • 0023188072 scopus 로고
    • Isolation of the alkane inducible cytochrome P450 (P450alk) gene from the yeast Candida tropicalis
    • Sanglard, D., C. Chen, and J. C. Loper. 1987. Isolation of the alkane inducible cytochrome P450 (P450alk) gene from the yeast Candida tropicalis. Biochem. Biophys. Res. Commun. 144:251-257.
    • (1987) Biochem. Biophys. Res. Commun , vol.144 , pp. 251-257
    • Sanglard, D.1    Chen, C.2    Loper, J.C.3
  • 38
    • 0028963304 scopus 로고
    • Yeast transcriptional activator INO2 interacts as an Ino2p/Ino4p basic helix-loop-helix heteromeric complex with the inositol/choline-responsive element necessary for expression of phospholipid biosynthetic genes in Saccharomyces cerevisiae
    • Schwank, S., R. Ebbert, K. Rautenstrauss, E. Schweizer, and H. J. Schuller. 1995. Yeast transcriptional activator INO2 interacts as an Ino2p/Ino4p basic helix-loop-helix heteromeric complex with the inositol/choline-responsive element necessary for expression of phospholipid biosynthetic genes in Saccharomyces cerevisiae. Nucleic Acids Res. 23:230-237.
    • (1995) Nucleic Acids Res , vol.23 , pp. 230-237
    • Schwank, S.1    Ebbert, R.2    Rautenstrauss, K.3    Schweizer, E.4    Schuller, H.J.5
  • 39
    • 0026676224 scopus 로고
    • Identification and characterization of additional members of the cytochrome P450 multigene family CYP52 of Candida tropicalis
    • Seghezzi, W., C. Meili, U. Ruffiner, R. Kuenzi, D. Sanglard, and A. Fiechter. 1992. Identification and characterization of additional members of the cytochrome P450 multigene family CYP52 of Candida tropicalis. DNA Cell Biol. 11:767-780.
    • (1992) DNA Cell Biol , vol.11 , pp. 767-780
    • Seghezzi, W.1    Meili, C.2    Ruffiner, U.3    Kuenzi, R.4    Sanglard, D.5    Fiechter, A.6
  • 40
    • 0026040423 scopus 로고
    • Characterization of a second alkane-inducible cytochrome P450-encoding gene, CYP52A2, from Candida tropicalis
    • Seghezzi, W., D. Sanglard, and A. Fiechter. 1991. Characterization of a second alkane-inducible cytochrome P450-encoding gene, CYP52A2, from Candida tropicalis. Gene 106:51-60.
    • (1991) Gene , vol.106 , pp. 51-60
    • Seghezzi, W.1    Sanglard, D.2    Fiechter, A.3
  • 41
    • 0029048826 scopus 로고
    • Mechanisms of membrane toxicity of hydrocarbons
    • Sikkema, J., J. A. de Bont, and B. Poolman. 1995. Mechanisms of membrane toxicity of hydrocarbons. Microbiol. Rev. 59:201-222.
    • (1995) Microbiol. Rev , vol.59 , pp. 201-222
    • Sikkema, J.1    de Bont, J.A.2    Poolman, B.3
  • 43
    • 0036289576 scopus 로고    scopus 로고
    • YIALK1 encoding the cytochrome P450ALK1 in Yarrowia lipolytica is transcriptionally induced by n-alkane through two distinct cis-elements on its promoter
    • Sumita, T., T. Iida, S. Yamagami, H. Horiuchi, M. Takagi, and A. Ohta. 2002. YIALK1 encoding the cytochrome P450ALK1 in Yarrowia lipolytica is transcriptionally induced by n-alkane through two distinct cis-elements on its promoter. Biochem. Biophys. Res. Commun. 294:1071-1078.
    • (2002) Biochem. Biophys. Res. Commun , vol.294 , pp. 1071-1078
    • Sumita, T.1    Iida, T.2    Yamagami, S.3    Horiuchi, H.4    Takagi, M.5    Ohta, A.6
  • 44
    • 0010228340 scopus 로고
    • 2nd ed, Academic Press. London. United Kingdom
    • Tanaka, A., and S. Fukui. 1989. The yeast. 2nd ed., vol. 3, p. 261-287. Academic Press. London. United Kingdom.
    • (1989) The yeast , vol.3 , pp. 261-287
    • Tanaka, A.1    Fukui, S.2
  • 45
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 46
    • 0028970090 scopus 로고
    • Structure and function of transcriptional activation domains
    • Triezenberg, S. J. 1995. Structure and function of transcriptional activation domains. Curr. Opin. Genet. Dev. 5:190-196.
    • (1995) Curr. Opin. Genet. Dev , vol.5 , pp. 190-196
    • Triezenberg, S.J.1
  • 47
    • 0025341295 scopus 로고
    • Mutations that disrupt DNA binding and dimer formation in the 1147 helix-loop-helix protein map to distinct domains
    • Voronova, A., and D. Baltimore. 1990. Mutations that disrupt DNA binding and dimer formation in the 1147 helix-loop-helix protein map to distinct domains. Proc. Natl. Acad. Sci. USA 87:4722-4726.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4722-4726
    • Voronova, A.1    Baltimore, D.2
  • 48
    • 0034936617 scopus 로고    scopus 로고
    • The negative regulator Opi1 of phospholipid biosynthesis in yeast contacts the pleiotropic repressor Sin3 and the transcriptional activator Ino2
    • Wagner, C., M. Dietz, J. Wittmann, A. Albrecht, and H. J. Schuller. 2001. The negative regulator Opi1 of phospholipid biosynthesis in yeast contacts the pleiotropic repressor Sin3 and the transcriptional activator Ino2. Mol. Microbiol. 41:155-166.
    • (2001) Mol. Microbiol , vol.41 , pp. 155-166
    • Wagner, C.1    Dietz, M.2    Wittmann, J.3    Albrecht, A.4    Schuller, H.J.5
  • 49
    • 0026088571 scopus 로고
    • The OPI1 gene of Saccharomyces cerevisiae, a negative regulator of phospholipid biosynthesis, encodes a protein containing polyglutumine tracts and a leucine zipper
    • White, M. J., J. P. Hirsch, and S. A. Henry. 1991. The OPI1 gene of Saccharomyces cerevisiae, a negative regulator of phospholipid biosynthesis, encodes a protein containing polyglutumine tracts and a leucine zipper. J. Biol. Chem. 266:863-872.
    • (1991) J. Biol. Chem , vol.266 , pp. 863-872
    • White, M.J.1    Hirsch, J.P.2    Henry, S.A.3
  • 50
    • 0033590619 scopus 로고    scopus 로고
    • Multiple p450alk (cytochrome P450 alkane hydroxylase) genes from the halotolerant yeast Debaryomyces hansenii
    • Yadav, J. S., and J. C. Loper. 1999. Multiple p450alk (cytochrome P450 alkane hydroxylase) genes from the halotolerant yeast Debaryomyces hansenii. Gene 226:139-146.
    • (1999) Gene , vol.226 , pp. 139-146
    • Yadav, J.S.1    Loper, J.C.2
  • 51
    • 0034805867 scopus 로고    scopus 로고
    • Isolation and characterization of acetoacetyl-CoA thiolase gene essential for n-decane assimilation in yeast Yarrowia lipolytica
    • Yamagami, S., T. Iida, Y. Nagata, A. Ohta, and M. Takagi. 2001. Isolation and characterization of acetoacetyl-CoA thiolase gene essential for n-decane assimilation in yeast Yarrowia lipolytica. Biochem. Biophys. Res. Commun. 282:832-838.
    • (2001) Biochem. Biophys. Res. Commun , vol.282 , pp. 832-838
    • Yamagami, S.1    Iida, T.2    Nagata, Y.3    Ohta, A.4    Takagi, M.5
  • 52
    • 2542431032 scopus 로고    scopus 로고
    • A basic helix-loop-helix transcription factor essential for cytochrome P450 induction in response to alkanes in yeast Yarrowia lipolytica
    • Yamagami, S., D. Morioka, R. Fukuda, and A. Ohta. 2004. A basic helix-loop-helix transcription factor essential for cytochrome P450 induction in response to alkanes in yeast Yarrowia lipolytica. J. Biol. Chem. 279:22183-22189.
    • (2004) J. Biol. Chem , vol.279 , pp. 22183-22189
    • Yamagami, S.1    Morioka, D.2    Fukuda, R.3    Ohta, A.4


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