메뉴 건너뛰기




Volumn 63, Issue 9, 1997, Pages 3341-3344

Effects of overproduction of the catalytic domain of 3-hydroxy-3- methylglutaryl coenzyme A reductase on squalene synthesis in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; MEVALONIC ACID; SQUALENE;

EID: 0030772492     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.63.9.3341-3344.1997     Document Type: Article
Times cited : (205)

References (18)
  • 1
    • 0023779728 scopus 로고
    • Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol biosynthesis
    • Basson, M. E., M. Thorsness, J. Finermoore, R. M. Stroud, and J. Rine. 1988. Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol biosynthesis. Mol. Cell. Biol. 8:3797-3808.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3797-3808
    • Basson, M.E.1    Thorsness, M.2    Finermoore, J.3    Stroud, R.M.4    Rine, J.5
  • 2
    • 0030029174 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methylglutaryl-coenzyme A reductase from Haloferax volcanii: Purification, characterization, and expression in Escherichia coli
    • Bischoff, K. M., and V. W. Rodwell. 1996. 3-Hydroxy-3-methylglutaryl-coenzyme A reductase from Haloferax volcanii: purification, characterization, and expression in Escherichia coli. J. Bacteriol. 178:19-23.
    • (1996) J. Bacteriol. , vol.178 , pp. 19-23
    • Bischoff, K.M.1    Rodwell, V.W.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0020078214 scopus 로고
    • Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase
    • Carlson, M., and D. Botstein. 1982. Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase. Cell 28:145-154.
    • (1982) Cell , vol.28 , pp. 145-154
    • Carlson, M.1    Botstein, D.2
  • 5
    • 0028336801 scopus 로고
    • Feedback-regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cerevisiae
    • Dimster-Denk, D., M. K. Thorsness, and J. Rine. 1994. Feedback-regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cerevisiae. Mol. Biol. Cell 5:655-665.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 655-665
    • Dimster-Denk, D.1    Thorsness, M.K.2    Rine, J.3
  • 6
    • 0029994476 scopus 로고    scopus 로고
    • Transcriptional regulation of a sterolbiosynthetic enzyme by sterol levels in Saccharomyces cerevisiae
    • Dimster-Denk, D., and J. Rine. 1996. Transcriptional regulation of a sterolbiosynthetic enzyme by sterol levels in Saccharomyces cerevisiae. Mol. Biol. Cell 16:3981-3989.
    • (1996) Mol. Biol. Cell , vol.16 , pp. 3981-3989
    • Dimster-Denk, D.1    Rine, J.2
  • 7
    • 0029917248 scopus 로고    scopus 로고
    • The biology of HMG-CoA reductase: The pros of contra-regulation
    • Hampton, R., D. Dimster-Denk, and J. Rine. 1996. The biology of HMG-CoA reductase: the pros of contra-regulation. Trends Biochem. Sci. 21:140-145.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 140-145
    • Hampton, R.1    Dimster-Denk, D.2    Rine, J.3
  • 8
    • 0028213166 scopus 로고
    • Regulated degradation of HMG-CoA. Reductase, an integral membrane-protein of the endoplasmic-reticulum, in yeast
    • Hampton, R. Y., and J. Rine. 1994. Regulated degradation of HMG-CoA. reductase, an integral membrane-protein of the endoplasmic-reticulum, in yeast. J. Cell Biol. 125:299-312.
    • (1994) J. Cell Biol. , vol.125 , pp. 299-312
    • Hampton, R.Y.1    Rine, J.2
  • 10
    • 0020804291 scopus 로고
    • Oxygen requirements for formation and activity of the squalene epoxidase in Saccharomyces cerevisiae
    • Jahnke, L., and H. P. Klein. 1983. Oxygen requirements for formation and activity of the squalene epoxidase in Saccharomyces cerevisiae. J. Bacteriol. 155:488-492.
    • (1983) J. Bacteriol. , vol.155 , pp. 488-492
    • Jahnke, L.1    Klein, H.P.2
  • 11
    • 0010293791 scopus 로고
    • Synthesis of lipids in resting cells of Saccharomyces cerevisiae
    • Klein, H. P. 1955. Synthesis of lipids in resting cells of Saccharomyces cerevisiae. J. Bacteriol. 69:620-627.
    • (1955) J. Bacteriol. , vol.69 , pp. 620-627
    • Klein, H.P.1
  • 12
    • 4244130653 scopus 로고
    • The synthesis of sterols in resting cells of Saccharomyces cerevisiae
    • Klein, H. P., N. R. Eaton, and J. C. Murphy. 1954. The synthesis of sterols in resting cells of Saccharomyces cerevisiae. Biochim. Biophys. Acta 13:591.
    • (1954) Biochim. Biophys. Acta , vol.13 , pp. 591
    • Klein, H.P.1    Eaton, N.R.2    Murphy, J.C.3
  • 13
    • 0024803720 scopus 로고
    • Regulation of squalene synthetase and squalene epoxidase activities in Saccharomyces cerevisiae
    • M'baya, B., M. Fegueur, M. Servouse, and F. Karst. 1989. Regulation of squalene synthetase and squalene epoxidase activities in Saccharomyces cerevisiae. Lipids 24:1020-1023.
    • (1989) Lipids , vol.24 , pp. 1020-1023
    • M'baya, B.1    Fegueur, M.2    Servouse, M.3    Karst, F.4
  • 14
    • 0023661340 scopus 로고
    • Antagonistic controls regulate copy number of the yeast 2-μm plasmid
    • Murray, J. A. H., M. Scarpa, N. Rossi, and G. Cesareni. 1987. Antagonistic controls regulate copy number of the yeast 2-μm plasmid. EMBO J. 6:4205-4212.
    • (1987) EMBO J. , vol.6 , pp. 4205-4212
    • Murray, J.A.H.1    Scarpa, M.2    Rossi, N.3    Cesareni, G.4
  • 15
    • 0018106855 scopus 로고
    • Metabolism of sterols in yeast
    • Parks, L. W. 1978. Metabolism of sterols in yeast. Crit. Rev. Microbiol. 6:301-341.
    • (1978) Crit. Rev. Microbiol. , vol.6 , pp. 301-341
    • Parks, L.W.1
  • 16
    • 0021891303 scopus 로고
    • Yeast sterols: Yeast mutants as tools for the study of sterol metabolism
    • Parks, L. W., D. K. Bottema, R. J. Rodriguez, and T. A. Lewis. 1978. Yeast sterols: yeast mutants as tools for the study of sterol metabolism. Methods Enzymol. 111:333-346.
    • (1978) Methods Enzymol. , vol.111 , pp. 333-346
    • Parks, L.W.1    Bottema, D.K.2    Rodriguez, R.J.3    Lewis, T.A.4
  • 17
    • 0029833459 scopus 로고    scopus 로고
    • Transcriptional regulation by ergosterol in the yeast Saccharomyces cerevisiae
    • Smith, S. J., J. H. Crowley, and J. Rine. 1996. Transcriptional regulation by ergosterol in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 16:5427-5432.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5427-5432
    • Smith, S.J.1    Crowley, J.H.2    Rine, J.3
  • 18
    • 0024306198 scopus 로고
    • Positive and negative transcriptional control by heme of genes encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cerevisiae
    • Thorsness, M., W. Schafer, L. D'Ari, and J. Rine. 1989. Positive and negative transcriptional control by heme of genes encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cerevisiae. Mol. Cell. Biol. 9:5702-5712.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5702-5712
    • Thorsness, M.1    Schafer, W.2    D'Ari, L.3    Rine, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.