PMID:3275612
| Citation |
Barr, K, Ward, S, Meier-Dieter, U, Mayer, H and Rick, PD (1988) Characterization of an Escherichia coli rff mutant defective in transfer of N-acetylmannosaminuronic acid (ManNAcA) from UDP-ManNAcA to a lipid-linked intermediate involved in enterobacterial common antigen synthesis. J. Bacteriol. 170:228-33 |
|---|---|
| Abstract |
The rff genes of Salmonella typhimurium include structural genes for enzymes involved in the conversion of UDP N-acetyl-D-glucosamine (UDP-GlcNAc) to UDP N-acetyl-D-mannosaminuronic acid (UDP-ManNAcA), the donor of ManNAcA residues in enterobacterial common antigen (ECA) synthesis. An rff mutation (rff-726) of Escherichia coli has been described (U. Meier and H. Mayer, J. Bacteriol. 163:756-762, 1985) that abolished ECA synthesis but which did not affect the synthesis of UDP-ManNAcA or any other components of ECA. The nature of the enzymatic defect resulting from the rff-726 lesion was investigated in the present study. The in vitro synthesis of GlcNAc-pyrophosphorylundecaprenol (lipid I), an early intermediate in ECA synthesis, was demonstrated by using membranes prepared from a mutant of E. coli possessing the rff-726 lesion. However, in vitro synthesis of the next lipid-linked intermediate in the biosynthetic sequence, ManNAcA-GlcNAc-pyrophosphorylundecaprenol (lipid II), was severely impaired. Transduction of wild-type rff genes into the mutant restored the ability to synthesize both lipid II and ECA as determined by in vitro assay and Western blot (immunoblot) analyses done with anti-ECA monoclonal antibody, respectively. Our results are consistent with the conclusion that the rff-726 mutation is located in the structural gene for the transferase that catalyzes the transfer of ManNAcA from UDP-ManNAcA to lipid I. |
| Links | |
| Keywords |
Antigens, Bacterial/biosynthesis; Antigens, Bacterial/genetics; Chemical Phenomena; Chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/immunology; Escherichia coli/metabolism; Genes; Genes, Bacterial; Hexosyltransferases/genetics; Hexosyltransferases/metabolism; Lipid Metabolism; Mutation; N-Acetylhexosaminyltransferases; Transduction, Genetic; Transferases/genetics; Transferases/metabolism; Uronic Acids/metabolism |
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