1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles

Journal of Biological Chemistry

Volumn 275, Issue 1, 2000, Pages 235-240

  Athenstaedt, Karin ^a   Daum, Günther ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; FUNGAL ENZYME; GLYCEROPHOSPHOLIPID; OXIDOREDUCTASE; PHOSPHATIDIC ACID;

AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; CELLULAR DISTRIBUTION; ENZYME ACTIVITY; FUNGUS SPORE; NONHUMAN; OPEN READING FRAME; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; YEAST;

AMINO ACID SEQUENCE; BASE SEQUENCE; CELL COMPARTMENTATION; CLONING, MOLECULAR; DATABASES, FACTUAL; ENDOPLASMIC RETICULUM; ESCHERICHIA COLI; GENE DELETION; GENES, FUNGAL; LIPID METABOLISM; MOLECULAR SEQUENCE DATA; OPEN READING FRAMES; ORGANELLES; PHENOTYPE; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS, PROTEIN; SEQUENCE HOMOLOGY, AMINO ACID; SUBCELLULAR FRACTIONS; SUGAR ALCOHOL DEHYDROGENASES;

ESCHERICHIA COLI; FUNGI; PROKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 0034614454     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.1.235     Document Type: Article

References (43)

1. Bishop, W. R., and Bell, R. M. (1988) Annu. Rev. Cell Biol. 4, 579-610
2. Van den Bosch, H. (1974) Annu. Rev. Biochem. 43, 243-277
3. Gurr, M. I. (1980) in The Biochemistry of Plants (Stumpf, P. K., ed.) Vol. 4, pp. 205-248, Academic Press, Inc., New York
4. Jones, C. L., and Hajra, A. K. (1980) J. Biol. Chem. 255, 8289-8295
5. Hajra, A. K. (1997) Biochim. Biophys. Acta 1348, 27-34
6. Johnston, J. M., and Paltauf, F. (1970) Biochim. Biophys. Acta 218, 431-440
7. Schlossman, D. M., and Bell, R. M. (1978) J. Bacteriol. 133, 1368-1376
8. Athenstaedt, K., Weys, S., Paltauf, F., and Daum, G. (1999) J. Bacteriol. 181, 1458-1463
9. Bell, R. M., and Coleman, R. A. (1983) in The Enzymes (Boyer, P. D., ed) Academic Press, Inc., New York
10. Christiansen, K. (1978) Biochim. Biophys. Acta 530, 78-90
11. Zinser, E., Sperka-Gottlieb, C. D. M., Fasch, E.-V., Kohlwein, S. D., Paltauf, F., and Daum, G. (1991) J. Bacteriol. 173, 2026-2034
12. Athenstaedt, K., and Daum, G. (1997) J. Bacteriol. 179, 7611-7616
13. Racenis, P. V., Lai, J. L., Das, A. K., Mullick, P. C., Hajra, A. K., and Greenberg, M. L. (1992) J. Bacteriol. 174, 5702-5710
14. Datta, S. C., Gosh, M. K., and Hajra, A. K. (1990) J. Biol. Chem. 265, 8268-8274
15. Oka, A., Sugisaki, H., and Takanami, M. (1981) J. Mol. Biol. 147, 217-226
16. Wach, A., Brachat, A., Pohlmann, R., and Phillipsen, P. (1994) Yeast 10, 1793-1808
17. Jimenez, A., and Davies, J. (1980) Nature 287, 869-871
18. Wach, A. (1996) Yeast 12, 259-265
19. Gietz, R. D., and Schiestl, R. H. (1995) Methods Mol. Cell. Biol. 5, 255-269
20. Huxley, C., Green, E. D., and Dunham, I. (1990) Trends Genet. 6, 236
21. Maniatis, T., Fritsch, E. F., and Sambrook, J. (1982) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
22. Leber, R., Zinser, E., Zellnig, G., Paltauf, F., and Daum, G. (1994) Yeast 10, 1421-1428
23. Zinser, E., and Daum, G. (1995) Yeast 11, 493-536
24. Laemmli, U. K. (1970) Nature 227, 680-685
25. Nagiec, M. M., Wells, G. B., Lester, R. L., and Dickson, R. C. (1993) J. Biol. Chem. 268, 22156-22163
26. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275
27. Haid, A., and Suissa, M. (1983) Methods Enzymol. 96, 192-205
28. Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Anal. Chem. 68, 850-858
29. Altschul, S. F., and Lipman, D. J. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 5509-5513
30. Bates, E. J., and Saggerson, E. D. (1979) Biochem. J. 182, 751-762
31. Folch, J., Lees M., and Sloane-Stanley, G. H. (1957) J. Biol. Chem. 226, 497-509
32. Broekhuyse, R. M. (1968) Biochim. Biophys. Acta 260, 449-459
33. Lewis, T. A., Rodriguez, R. J., and Parks, L. W. (1987) Biochim. Biophys. Acta 921, 205-212
34. Xu, S., Norton, R. A., Crumley, F. G., and Nes, W. D. (1988) J. Chromatogr. 452, 377-398
35. Patterson, G. W. (1971) Anal. Chem. 43, 1165-1170
36. Morrison, W. R., and Smith, L. M. (1964) J. Lipid Res. 5, 600-608
37. Athenstaedt, K., Zweytick, D., Jandrositz, A., Kohlwein, S. D., and G. Daum, G. (1999) J. Bacteriol. 181, 6441-6448
38. Kyte, J., and Doolittle, R. F. (1982) J. Mol. Biol. 157, 105-132
39. Leber, R., Landl, K., Zinser, E., Ahorn, H., Spök, A., Kohlwein, S. D., Turnowsky, F., and Daum, G. (1998) Mol. Biol. Cell 9, 375-386
40. Snyder, F., Lee, T. C., and Wykle, R. L. (1985) in The Enzymes of Biological Membranes (Martonosi, A. N., ed) Vol. 2, pp. 1-58, Plenum Publishing Corp., New York
41. Gaigg, B., Simbeni, R., Hrastnik, C., Paltauf, F., and Daum G. (1995) Biochim. Biophys. Acta 1234, 214-220
42. Achleitner, G., Gaigg, B., Krasser, A., Kaineredorfer, E., Kohlwein, S. D., Perktold, A., Zellnig, G., and Daum, G. (1999) Eur. J. Biochem. 264, 545-553
43. Schneiter, R., Brügger, B., Zellnig, G., Leber, A., Eder, S., Lampl, M., Athenstaedt, K., Hrastnik. C., Sandhoff, R., Daum, G., Paltauf, F., Wieland, F. T., and Kohlwein, S. D. (1999) J. Cell Biol. 146, 714-754