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Mutants of Escherichia coli Defective in Membrane Phospholipid Synthesis: Mapping of sn-Glycerol 3-Phosphate Acyltransferase K_m Mutants

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, and Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710

ABSTRACT

plsB mutants of Escherichia coli are sn-glycerol 3-phosphate auxotrophs which owe their requirement to a K_m defect in sn-glycerol 3-phosphate acyltransferase, the first enzyme in the phospholipid biosynthetic pathway. We have located the plsB gene at minute 69 of the E. coli genetic map, far removed from the gene defined by mutants with a temperature-sensitive sn-glycerol 3-phosphate acyltransferase. The plsB gene was cotransduced with the dctA locus, and the transduction data indicated that the clockwise gene order is asd, plsB, dctA, xyl. plsB^– is recessive to plsB⁺ and all acyltransferase K_m mutants tested lie very close to the plsB locus. Effective supplementation of plsB mutants was shown not to require a defective glpD gene.

This article has been cited by other articles:

• Heath, R. J., Rock, C. O. (1999). A Missense Mutation Accounts for the Defect in the Glycerol-3-Phosphate Acyltransferase Expressed in the plsB26 Mutant. J. Bacteriol. 181: 1944-1946 [Abstract] [Full Text]  
• Heath, R. J., Rock, C. O. (1998). A Conserved Histidine Is Essential for Glycerolipid Acyltransferase Catalysis. J. Bacteriol. 180: 1425-1430 [Abstract] [Full Text]