HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tillman, T. S. Articles by Bell, R. M. Search for Related Content PubMed PubMed Citation Articles by Tillman, T. S. Articles by Bell, R. M. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 261, Issue 20, 9144-9149, Jul, 1986

Mutants of Saccharomyces cerevisiae defective in sn-glycerol-3- phosphate acyltransferase. Simultaneous loss of dihydroxyacetone phosphate acyltransferase indicates a common gene

TS Tillman and RM Bell

Fourteen independent mutants of Saccharomyces cerevisiae defective in sn-glycerol-3-phosphate acyltransferase activity were isolated using a colony autoradiographic screening technique. All 14 mutants were similarly defective in dihydroxyacetone phosphate acyltransferase activity. The mutations were recessive and fell into a single complementation group. Tetrad analysis gave results consistent with mutations in a single nuclear gene affecting both activities. sn- Glycerol-3-phosphate acyltransferase activity from different mutant strains exhibited different substrate dependencies and differing responses to temperature, detergent, and pH. In each case, the response of the dihydroxyacetone phosphate acyltransferase activity was similar to that of the sn-glycerol-3-phosphate acyltransferase. These results are consistent with the mutations occurring in the structural gene. The data also establish that the predominant dihydroxyacetone phosphate acyltransferase activity in yeast is a second activity of the sn- glycerol-3-phosphate acyltransferase.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				K. Stalberg, A. C. Neal, H. Ronne, and U. Stahl Identification of a novel GPCAT activity and a new pathway for phosphatidylcholine biosynthesis in S. cerevisiae J. Lipid Res., August 1, 2008; 49(8): 1794 - 1806. [Abstract] [Full Text] [PDF]

				T. C. Santiago, R. Zufferey, R. S. Mehra, R. A. Coleman, and C. B. Mamoun The Plasmodium falciparum PfGatp is an Endoplasmic Reticulum Membrane Protein Important for the Initial Step of Malarial Glycerolipid Synthesis J. Biol. Chem., March 5, 2004; 279(10): 9222 - 9232. [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]

				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]

				K. Athenstaedt, S. Weys, F. Paltauf, and G. Daum Redundant Systems of Phosphatidic Acid Biosynthesis via Acylation of Glycerol-3-Phosphate or Dihydroxyacetone Phosphate in the Yeast Saccharomyces cerevisiae J. Bacteriol., March 1, 1999; 181(5): 1458 - 1463. [Abstract] [Full Text]