Membrane phospholipid synthesis in Escherichia coli. Identification of the sn-glycerol-3-phosphate acyltransferase polypeptide as the plsB gene product. 1980

T J Larson, and V A Lightner, and P R Green, and P Modrich, and R M Bell

A collection of hybrid plasmids bearing a structural gene, plsB, for the sn-glycerol-3-phosphate acyltransferase of Escherichia cole (Lightner, V. A., Larson, T. J., Tailleur, P., Kantor, G. D., Raetz, C. R. H., Bell, R. M., and Modrich, P. (1980) J. Biol. Chem. 255, 9413-9420) was employed to identify the membrane protein which is the sn-glycerol-3-phosphate acyltransferase. Strains containing these hybrid plasmids exhibited a marked increase in sn-glycerol-3-phosphate acyltransferase activity which was quantitatively extracted from membrane preparations with Triton X-100. Analysis of polypeptides present in detergent extracts of membranes from strains harboring the hybrid plasmids revealed a marked overproduction of a protein with an apparent molecular weight of 83,000, which was also the major protein labeled in minicells containing these hybrid plasmids. The labeled 83,000-dalton protein cochromatographed with sn-glycerol-3-phosphate acyltransferase activity on DEAE-cellulose. Utilization of three hybrid plasmids bearing amber mutations within the plsB gene demonstrated that the 83,000-dalton protein is the sn-glycerol-3-phosphate acyltransferase. Analysis of Bam HI deletion plasmids demonstrated that a 2.3-megadalton DNA fragment is necessary and sufficient for expression of the plsB gene. The sn-glycerol-3-phosphate acyltransferase was purified to near homogeneity from Triton X-100 extracts of membranes from overproducing strains. The preparations had reconstitutable specific activity of 2.5 micromol/min/mg and contained a single polypeptide with an apparent molecular weight of 83,000.

UI MeSH Term Description Entries
D008563 Membrane Lipids Lipids, predominantly phospholipids, cholesterol and small amounts of glycolipids found in membranes including cellular and intracellular membranes. These lipids may be arranged in bilayers in the membranes with integral proteins between the layers and peripheral proteins attached to the outside. Membrane lipids are required for active transport, several enzymatic activities and membrane formation. Cell Membrane Lipid,Cell Membrane Lipids,Membrane Lipid,Lipid, Cell Membrane,Lipid, Membrane,Lipids, Cell Membrane,Lipids, Membrane,Membrane Lipid, Cell,Membrane Lipids, Cell
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010743 Phospholipids Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system. Phosphatides,Phospholipid
D010957 Plasmids Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS. Episomes,Episome,Plasmid
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005796 Genes A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms. Cistron,Gene,Genetic Materials,Cistrons,Genetic Material,Material, Genetic,Materials, Genetic
D005838 Genotype The genetic constitution of the individual, comprising the ALLELES present at each GENETIC LOCUS. Genogroup,Genogroups,Genotypes
D005992 Glycerol-3-Phosphate O-Acyltransferase An enzyme that transfers acyl groups from acyl-CoA to glycerol-3-phosphate to form monoglyceride phosphates. It acts only with CoA derivatives of fatty acids of chain length above C-10. Also forms diglyceride phosphates. EC 2.3.1.15. Glycerolphosphate Acyltransferase,Stearyl-CoA Glycerophosphate Transstearylase,Acyl-CoA Sn-Glycerol-3-Phosphate-O-Acyltransferase,Glycerophosphate Acyltransferase,Acyl CoA Sn Glycerol 3 Phosphate O Acyltransferase,Acyltransferase, Glycerolphosphate,Acyltransferase, Glycerophosphate,Glycerol 3 Phosphate O Acyltransferase,Glycerophosphate Transstearylase, Stearyl-CoA,O-Acyltransferase, Glycerol-3-Phosphate,Sn-Glycerol-3-Phosphate-O-Acyltransferase, Acyl-CoA,Stearyl CoA Glycerophosphate Transstearylase,Transstearylase, Stearyl-CoA Glycerophosphate
D000217 Acyltransferases Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3. Acyltransferase

Related Publications

T J Larson, and V A Lightner, and P R Green, and P Modrich, and R M Bell
November 1981, The Journal of biological chemistry,
T J Larson, and V A Lightner, and P R Green, and P Modrich, and R M Bell
October 1974, Journal of bacteriology,
T J Larson, and V A Lightner, and P R Green, and P Modrich, and R M Bell
September 1997, Biochimica et biophysica acta,
T J Larson, and V A Lightner, and P R Green, and P Modrich, and R M Bell
March 1974, Journal of bacteriology,
T J Larson, and V A Lightner, and P R Green, and P Modrich, and R M Bell
July 1989, The Journal of biological chemistry,
T J Larson, and V A Lightner, and P R Green, and P Modrich, and R M Bell
December 1997, Journal of bacteriology,
T J Larson, and V A Lightner, and P R Green, and P Modrich, and R M Bell
February 1987, Journal of bacteriology,
T J Larson, and V A Lightner, and P R Green, and P Modrich, and R M Bell
December 1984, The Journal of biological chemistry,
T J Larson, and V A Lightner, and P R Green, and P Modrich, and R M Bell
October 1994, The Journal of biological chemistry,
Copied contents to your clipboard!