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Literature DB >> 368018

Incorporation of phosphatidylglycerol into murein lipoprotein in intact cells of Salmonella typhimurium by phospholipid vesicle fusion.

Abstract

The biosynthesis of the diglyceride moiety of murein lipoprotein was studied by fusion of labeled phospholipid vesicles with intact cells of Salmonella typhimurium. Phosphatidylglycerol was found to be an excellent donor for the glyceryl moiety in lipoprotein, whereas phosphatidylethanolamine and cardiolipin were not. The incorporation of radioactivity from monoacyl-phosphatidylglycerol into lipoprotein can be attributed to its conversion to phosphatidylglycerol. The results strongly support our hypothesis that the glyceryl residue covalently linked to murein lipoprotein is derived from the nonacylated glycerol moiety of phosphatidylglycerol.

Entities: Chemical Species

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Year: 1979 PMID： 368018 PMCID： PMC218451 DOI： 10.1128/jb.137.1.309-312.1979

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

16 in total

1. Studies on the biosynthesis of acylphosphatidylglycerol in Escherichia coli B and B/r.

Authors: K S Cho; S D Hong; J M Cho; C S Chang; K S Lee
Journal: Biochim Biophys Acta Date: 1976-01-18

2. Lipid deficiency in a lipoprotein mutant of Escherichia coli.

Authors: H Rotering; V Braun
Journal: FEBS Lett Date: 1977-11-01 Impact factor: 4.124

3. Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murein-lipoprotein of the Escherichia coli outer membrane.

Authors: K Hantke; V Braun
Journal: Eur J Biochem Date: 1973-04

Review 3. Lipoproteins in bacteria.

Authors: S Hayashi; H C Wu
Journal: J Bioenerg Biomembr Date: 1990-06 Impact factor: 2.945

4. Transfer of phosphoethanolamine residues from phosphatidylethanolamine to the membrane-derived oligosaccharides of Escherichia coli.

Authors: K J Miller; E P Kennedy
Journal: J Bacteriol Date: 1987-02 Impact factor: 3.490

9. Incorporation of acyl moieties of phospholipids into murein lipoprotein in intact cells of Escherichia coli by phospholipid vesicle fusion.

Authors: J S Lai; H C Wu
Journal: J Bacteriol Date: 1980-10 Impact factor: 3.490

9 in total

Incorporation of phosphatidylglycerol into murein lipoprotein in intact cells of Salmonella typhimurium by phospholipid vesicle fusion.

1. Studies on the biosynthesis of acylphosphatidylglycerol in Escherichia coli B and B/r.

2. Lipid deficiency in a lipoprotein mutant of Escherichia coli.

3. Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murein-lipoprotein of the Escherichia coli outer membrane.

4. Acyl phosphatidylglycerol. A new phospholipid from Salmonella typhimurium.

5. Biosynthesis and assembly of envelope lipoprotein in a glycerol-requiring mutant of Salmonella typhimurium.

6. Mechanism of the enzymatic synthesis of cardiolipin in Escherichia coli.

7. Biosynthesis of the covalently linked diglyceride in murein lipoprotein of Escherichia coli.

8. Phospholipid metabolism during bacterial growth.

9. Amino acid replacement in a mutant lipoprotein of the Escherichia coli outer membrane.

10. Translocation of phospholipids between the outer and inner membranes of Salmonella typhimurium.

1. Covalent linkage of polyamines to peptidoglycan in Anaerovibrio lipolytica.

Review 2. Post-translational modification and processing of outer membrane prolipoproteins in Escherichia coli.

Review 3. Lipoproteins in bacteria.

4. Transfer of phosphoethanolamine residues from phosphatidylethanolamine to the membrane-derived oligosaccharides of Escherichia coli.

5. Fatty acid metabolism in sn-glycerol-3-phosphate acyltransferase (plsB) mutants.

6. Isolation and characterization of outer and inner membranes of Selenomonas ruminantium: lipid compositions.

7. Outer membrane proteins and cell surface structure of Selenomonas ruminantium.

8. Transfer of the phosphatidyl moiety of phosphatidylglycerol to phosphatidylethanolamine in Escherichia coli.

9. Incorporation of acyl moieties of phospholipids into murein lipoprotein in intact cells of Escherichia coli by phospholipid vesicle fusion.