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Volumn 70, Issue 11, 2006, Pages 2604-2612

Ternary complex formation of Ino2p-Ino4p transcription factors and Apl2p adaptin β subunit in yeast

Author keywords

Adaptin; Carbon source; Inositol biosynthesis; Oxidative stress; Transcriptional regulation

Indexed keywords

BIOSYNTHESIS; CARBON; CELLS; FERMENTATION; GENES; GLYCOLS; OXIDATION;

EID: 33751419240     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60146     Document Type: Article
Times cited : (4)

References (27)
  • 2
    • 0024494204 scopus 로고
    • Biosynthesis of inositol in yeast: Primary structure of myo-inositol-1-phosphate synthase (EC 5.5.1.4) and functional analysis of its structural gene, the INO1 locus
    • Dean-Johnson, M., and Henry, S., Biosynthesis of inositol in yeast: primary structure of myo-inositol-1-phosphate synthase (EC 5.5.1.4) and functional analysis of its structural gene, the INO1 locus. J. Biol. Chem., 264, 1274-1283 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 1274-1283
    • Dean-Johnson, M.1    Henry, S.2
  • 3
    • 0025848024 scopus 로고
    • Isolation and characterization of two distinct myo-inositol transport genes of Saccharomyces cerevisiae
    • Nikawa, J., Tsukagoshi, Y., and Yamashita, S., Isolation and characterization of two distinct myo-inositol transport genes of Saccharomyces cerevisiae. J. Biol. Chem., 266, 11184-11191 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 11184-11191
    • Nikawa, J.1    Tsukagoshi, Y.2    Yamashita, S.3
  • 4
    • 0026027643 scopus 로고
    • Identification of the upstream activation sequences responsible for the expression and regulation of the PEM1 and PEM2 genes encoding the enzymes of the phosphatidylethanolamine methylation pathway in Saccharomyces cerevisiae
    • Kodaki, T., Hosaka, K., Nikawa, J., and Yamashita, S., Identification of the upstream activation sequences responsible for the expression and regulation of the PEM1 and PEM2 genes encoding the enzymes of the phosphatidylethanolamine methylation pathway in Saccharomyces cerevisiae. J. Biochem., 109, 276-287 (1991).
    • (1991) J. Biochem. , vol.109 , pp. 276-287
    • Kodaki, T.1    Hosaka, K.2    Nikawa, J.3    Yamashita, S.4
  • 5
    • 0025755893 scopus 로고
    • Analysis of sequences in the INO1 promoter that are involved in its regulation by phospholipid precursors
    • Lopes, J. M., Hirsch, J. P., Chorgo, P. A., Schulze, K. L., and Henry, S. A., Analysis of sequences in the INO1 promoter that are involved in its regulation by phospholipid precursors. Nucleic Acids Res., 19, 1687-1693 (1991).
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1687-1693
    • Lopes, J.M.1    Hirsch, J.P.2    Chorgo, P.A.3    Schulze, K.L.4    Henry, S.A.5
  • 6
    • 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 Henry, S. A., 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).
    • (1994) J. Biol. Chem. , vol.269 , pp. 15344-15349
    • Ambroziak, J.1    Henry, S.A.2
  • 7
    • 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., Ebbert, R., Bautenstrauss, K., Schweizer, E., and Schuller, H.-J., 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).
    • (1995) Nucleic Acids Res. , vol.23 , pp. 230-237
    • Schwank, S.1    Ebbert, R.2    Bautenstrauss, K.3    Schweizer, E.4    Schuller, H.-J.5
  • 8
    • 0028876869 scopus 로고
    • Autoregulated expression of the yeast INO2 and INO4 helix-loop-helix activator genes effects cooperative regulation on their target genes
    • Ashburner, B. P., and Lopes, J. M., Autoregulated expression of the yeast INO2 and INO4 helix-loop-helix activator genes effects cooperative regulation on their target genes. Mol. Cell. Biol., 15, 1709-1715 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1709-1715
    • Ashburner, B.P.1    Lopes, J.M.2
  • 9
    • 0020287589 scopus 로고
    • Regulatory mutations of inositol biosynthesis in yeast: Isolation of inositol-excreting mutants
    • Greenberg, M. L., Reiner, B., and Henry, S. A., Regulatory mutations of inositol biosynthesis in yeast: isolation of inositol-excreting mutants. Genetics, 100, 19-33 (1982).
    • (1982) Genetics , vol.100 , pp. 19-33
    • Greenberg, M.L.1    Reiner, B.2    Henry, S.A.3
  • 10
    • 2942677427 scopus 로고    scopus 로고
    • Phospholipid metabolism regulated by a transcription factor sensing phosphatidic acid
    • Loewen, C. J. R., Gaspar, M. L., Jesch, S. A., Delon, C., Ktistakis, N. T., Henry, S. A., and Levine, T. P., Phospholipid metabolism regulated by a transcription factor sensing phosphatidic acid. Science, 304, 1644-1647 (2004).
    • (2004) Science , vol.304 , pp. 1644-1647
    • Loewen, C.J.R.1    Gaspar, M.L.2    Jesch, S.A.3    Delon, C.4    Ktistakis, N.T.5    Henry, S.A.6    Levine, T.P.7
  • 12
    • 0035158494 scopus 로고    scopus 로고
    • Adaptins: The final recount
    • Boehm, M., and Bonifacino, J. S., Adaptins: the final recount. Mol. Biol. Cell, 12, 2907-2920 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2907-2920
    • Boehm, M.1    Bonifacino, J.S.2
  • 13
    • 0028904692 scopus 로고
    • Saccharomyces cerevisiae Apl2p, a homologue of the mammalian clathrin AP β subunit, plays a role in clathrin-dependent Golgi functions
    • Rad, M. R., Phan, H. L., Kirchrath, L., Tan, P. K., Kirchhausen, T., Hollenberg, C. P., and Payne, G. S., Saccharomyces cerevisiae Apl2p, a homologue of the mammalian clathrin AP β subunit, plays a role in clathrin-dependent Golgi functions. J. Cell Sci., 108, 1605-1615 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 1605-1615
    • Rad, M.R.1    Phan, H.L.2    Kirchrath, L.3    Tan, P.K.4    Kirchhausen, T.5    Hollenberg, C.P.6    Payne, G.S.7
  • 14
    • 0037139604 scopus 로고    scopus 로고
    • Genetic analysis of adaptin function from yeast to mammals
    • Boehm, M., and Bonifacino, J. S., Genetic analysis of adaptin function from yeast to mammals. Gene, 286, 175-186 (2002).
    • (2002) Gene , vol.286 , pp. 175-186
    • Boehm, M.1    Bonifacino, J.S.2
  • 15
    • 0034903514 scopus 로고    scopus 로고
    • Clathrin interactions with C-terminal regions of the yeast AP-1 β and γ subunits are important for AP-1 association with clathrin coats
    • Yeung, B. G., and Payne, G. S., Clathrin interactions with C-terminal regions of the yeast AP-1 β and γ subunits are important for AP-1 association with clathrin coats. Traffic, 2, 565-576 (2001).
    • (2001) Traffic , vol.2 , pp. 565-576
    • Yeung, B.G.1    Payne, G.S.2
  • 18
    • 0018902403 scopus 로고
    • Regulation of phosphatidylethanolamine methyltransferase level by myo-inositol in Saccharomyces cerevisiae
    • Yamashita, S., and Oshima, A., Regulation of phosphatidylethanolamine methyltransferase level by myo-inositol in Saccharomyces cerevisiae. Eur. J. Biochem., 104, 611-616 (1980).
    • (1980) Eur. J. Biochem. , vol.104 , pp. 611-616
    • Yamashita, S.1    Oshima, A.2
  • 19
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K., and Kimura, A., Transformation of intact yeast cells treated with alkali cations. J. Bacteriol., 153, 163-168 (1983).
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 20
    • 0032004379 scopus 로고    scopus 로고
    • PCR- and ligation-mediated synthesis of marker cassettes with long flanking homology regions for gene disruption in Saccharomyces cerevisiae
    • Nikawa, J., and Kawabata, M., PCR- and ligation-mediated synthesis of marker cassettes with long flanking homology regions for gene disruption in Saccharomyces cerevisiae. Nucleic Acids Res., 26, 860-861 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 860-861
    • Nikawa, J.1    Kawabata, M.2
  • 21
    • 0026548118 scopus 로고
    • A dominant mutation that alters the regulation of INO1 expression in Saccharomyces cerevisiae
    • Hosaka, K., Nikawa, J., Kodaki, T., and Yamashita, S., A dominant mutation that alters the regulation of INO1 expression in Saccharomyces cerevisiae. J. Biochem., 111, 352-358 (1992).
    • (1992) J. Biochem. , vol.111 , pp. 352-358
    • Hosaka, K.1    Nikawa, J.2    Kodaki, T.3    Yamashita, S.4
  • 22
    • 3242757258 scopus 로고
    • Isolation and characterization of genes that promote the expression of inositol transporter gene ITR1 in Saccharomyces cerevisiae
    • Nikawa, J., and Hosaka, K., Isolation and characterization of genes that promote the expression of inositol transporter gene ITR1 in Saccharomyces cerevisiae. Mol. Microbiol., 10, 955-961 (1995).
    • (1995) Mol. Microbiol. , vol.10 , pp. 955-961
    • Nikawa, J.1    Hosaka, K.2
  • 23
    • 0141957388 scopus 로고    scopus 로고
    • Mutational analysis and location of the inositol transporters of Saccharomyces cerevisiae
    • Miyashita, M., Syugyo, M., and Nikawa, J., Mutational analysis and location of the inositol transporters of Saccharomyces cerevisiae. J. Biosci. Bioeng., 96, 291-297 (2003).
    • (2003) J. Biosci. Bioeng. , vol.96 , pp. 291-297
    • Miyashita, M.1    Syugyo, M.2    Nikawa, J.3
  • 24
    • 0032439653 scopus 로고    scopus 로고
    • Oxidative stress responses of the yeast Saccharomyces cerevisiae
    • Jamieson, D. J., Oxidative stress responses of the yeast Saccharomyces cerevisiae. Yeast, 14, 1511-1527 (1998).
    • (1998) Yeast , vol.14 , pp. 1511-1527
    • Jamieson, D.J.1
  • 25
    • 20444415235 scopus 로고    scopus 로고
    • Complex cellular responses to reactive oxygen species
    • Temple, M. D., Perrone, G. G., and Dawes, I. W., Complex cellular responses to reactive oxygen species. Trends Cell. Biol., 15, 319-326 (2005).
    • (2005) Trends Cell. Biol. , vol.15 , pp. 319-326
    • Temple, M.D.1    Perrone, G.G.2    Dawes, I.W.3
  • 26
    • 10444257943 scopus 로고    scopus 로고
    • Yeast signaling pathways in the oxidative stress response
    • Ikner, A., and Shiozaki, K., Yeast signaling pathways in the oxidative stress response. Mutat. Res., 569, 13-27 (2005).
    • (2005) Mutat. Res. , vol.569 , pp. 13-27
    • Ikner, A.1    Shiozaki, K.2
  • 27
    • 2342487990 scopus 로고    scopus 로고
    • Cells have distinct mechanisms to maintain protection against different reactive oxygen species: Oxidative-stress-response genes
    • Thorpe, G. W., Fong, C. S., Alic, N., Higgins, V. J., and Dawes, I. W., Cells have distinct mechanisms to maintain protection against different reactive oxygen species: oxidative-stress-response genes. Proc. Natl. Acad. Sci. USA, 101, 6564-6569 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6564-6569
    • Thorpe, G.W.1    Fong, C.S.2    Alic, N.3    Higgins, V.J.4    Dawes, I.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.