title: sn-glycerol-3-phosphate acyltransferase tubule formation is dependent upon heat shock proteins (htpR).
abstract: Overexpression of the Escherichia coli sn-glycerol-3-phosphate (glycerol-P) acyltransferase, an integral membrane protein, causes formation of ordered arrays of the enzyme in vitro. The formation of these tubular structures did not occur in an E. coli strain bearing a mutation in the htpR gene, the regulatory gene for the heat shock response. The htpR165 mutation was shown by genetic analysis to be the lesion responsible for blockage of tubule formation. Similar amounts of glycerol-P acyltransferase were produced in isogenic htpR+ and htpR165 strains, ruling out an effect of htpR165 on expression of glycerol-P acyltransferase. Further, phospholipid metabolism was not altered in either strain after induction of glycerol-P acyltransferase synthesis. Increased glycerol-P acyltransferase synthesis caused a partial induction of the heat shock response which was dependent upon a wild type htpR gene. The heat shock proteins induced were identified as the groEL and dnaK gene products on two-dimensional gels. These two proteins have been implicated in the assembly of bacteriophage coats. These heat shock proteins appear essential for tubule formation.
mesh_terms: D000217:Acyltransferases / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000648:ultrastructure*; D005796:Genes; D005798:Genes, Bacterial; D005809:Genes, Regulator; D005838:Genotype; D005992:Glycerol-3-Phosphate O-Acyltransferase / Q000235:genetics* / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000235:genetics / Q000502:physiology*; D008854:Microscopy, Electron; D009154:Mutation; D013045:Species Specificity
chemical_list: D006360:Heat-Shock Proteins; D000217:Acyltransferases; D005992:Glycerol-3-Phosphate O-Acyltransferase