|
|
|
|||||||
|
|||||||||
J Biol Chem, Vol. 275, Issue 1, 235-240, January 7, 2000
From the Institut für Biochemie und Lebensmittelchemie,
Technische Universität and Spezialforschungsbereich Biomembrane
Research Center, Petersgasse 12/2, A-8010 Graz, Austria
Biosynthesis of phosphatidic acid through the
dihydroxyacetone phosphate pathway requires NADPH-dependent
reduction of the intermediate 1-acyldihydroxyacetone phosphate before
the second step of acylation. Studies with isolated subcellular
fractions of the yeast Saccharomyces cerevisiae revealed
that lipid particles and the endoplasmic reticulum harbor
1-acyldihydroxyacetone-phosphate reductase (ADR) activity. Deletion of
the open reading frame YIL124w (in the following named
AYR1) abolished reduction of 1-acyldihydroxyacetone phosphate in lipid particles, whereas ADR activity in microsomes of the
deletion strain was decreased approximately 3-fold as compared with the
wild-type level. This result indicates that (i) both lipid particles
and microsomes harbor Ayr1p, which was confirmed by immunological
detection of the protein in these two cellular compartments, and (ii)
microsomes contain at least one additional ADR activity. As a
consequence of this redundancy, deletion of AYR1 neither
results in an obvious growth phenotype nor affects the lipid
composition of a haploid deletion strain. When a heterozygous AYR1+/ayr1
1-Acyldihydroxyacetone-phosphate Reductase (Ayr1p) of the Yeast
Saccharomyces cerevisiae Encoded by the Open Reading Frame
YIL124w Is a Major Component of Lipid Particles*
diploid strain
was subjected to sporulation; however, spores bearing the ayr1
defect failed to germinate, suggesting that Ayr1p plays an
essential role at this stage. Overexpression of Ayr1p at a 5- to
10-fold level of wild type caused growth arrest. Heterologous expression of Ayr1p in Escherichia coli resulted in gain of
ADR activity in the prokaryote, confirming that YIL124w is the
structural gene of the enzyme and does not encode a regulatory or
auxiliary component required for reduction of 1-acyldihydroxyacetone
phosphate. Taken together, these results identified Ayr1p of the yeast
as the first ADR from any organism at the molecular level.
*
This work was financially supported by the Fonds zur
Förderung der Wissenschaftlichen Forschung in Österreich
(projects 11491 and F706), the Austrian Ministry of Science and
Transportation (project 950080), and EUROFAN project BIO-CT95-0080.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 43-316-873-6462;
Fax: 43-316-873-6952; E-mail: f548daum@mbox.tu-graz.ac.at.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  E. V. Entchev, D. Schwudke, V. Zagoriy, V. Matyash, A. Bogdanova, B. Habermann, L. Zhu, A. Shevchenko, and T. V. Kurzchalia LET-767 Is Required for the Production of Branched Chain and Long Chain Fatty Acids in Caenorhabditis elegans J. Biol. Chem., June 20, 2008; 283(25): 17550 - 17560. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Zufferey and C. B. Mamoun Leishmania major Expresses a Single Dihydroxyacetone Phosphate Acyltransferase Localized in the Glycosome, Important for Rapid Growth and Survival at High Cell Density and Essential for Virulence J. Biol. Chem., March 24, 2006; 281(12): 7952 - 7959. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. J. Proszynski, R. W. Klemm, M. Gravert, P. P. Hsu, Y. Gloor, J. Wagner, K. Kozak, H. Grabner, K. Walzer, M. Bagnat, et al. A genome-wide visual screen reveals a role for sphingolipids and ergosterol in cell surface delivery in yeast PNAS, December 13, 2005; 102(50): 17981 - 17986. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M T Rae, D Niven, A Ross, T Forster, R Lathe, H O D Critchley, P Ghazal, and S G Hillier Steroid signalling in human ovarian surface epithelial cells: the response to interleukin-1{alpha} determined by microarray analysis J. Endocrinol., October 1, 2004; 183(1): 19 - 28. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Sorger, K. Athenstaedt, C. Hrastnik, and G. Daum A Yeast Strain Lacking Lipid Particles Bears a Defect in Ergosterol Formation J. Biol. Chem., July 23, 2004; 279(30): 31190 - 31196. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Athenstaedt and G. Daum YMR313c/TGL3 Encodes a Novel Triacylglycerol Lipase Located in Lipid Particles of Saccharomyces cerevisiae J. Biol. Chem., June 20, 2003; 278(26): 23317 - 23323. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
V. Zaremberg and C. R. McMaster Differential Partitioning of Lipids Metabolized by Separate Yeast Glycerol-3-phosphate Acyltransferases Reveals That Phospholipase D Generation of Phosphatidic Acid Mediates Sensitivity to Choline-containing Lysolipids and Drugs J. Biol. Chem., October 4, 2002; 277(41): 39035 - 39044. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Han, K. Gable, S. D. Kohlwein, F. Beaudoin, J. A. Napier, and T. M. Dunn The Saccharomyces cerevisiae YBR159w Gene Encodes the 3-Ketoreductase of the Microsomal Fatty Acid Elongase J. Biol. Chem., September 13, 2002; 277(38): 35440 - 35449. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Beaudoin, K. Gable, O. Sayanova, T. Dunn, and J. A. Napier A Saccharomyces cerevisiae Gene Required for Heterologous Fatty Acid Elongase Activity Encodes a Microsomal beta -Keto-reductase J. Biol. Chem., March 22, 2002; 277(13): 11481 - 11488. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z. Zheng and J. Zou The Initial Step of the Glycerolipid Pathway. IDENTIFICATION OF GLYCEROL 3-PHOSPHATE/DIHYDROXYACETONE PHOSPHATE DUAL SUBSTRATE ACYLTRANSFERASES IN SACCHAROMYCES CEREVISIAE J. Biol. Chem., November 2, 2001; 276(45): 41710 - 41716. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. Milla, K. Athenstaedt, F. Viola, S. Oliaro-Bosso, S. D. Kohlwein, G. Daum, and G. Balliano Yeast Oxidosqualene Cyclase (Erg7p) Is a Major Component of Lipid Particles J. Biol. Chem., January 18, 2002; 277(4): 2406 - 2412. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |