Initial membrane reaction in peptidoglycan synthesis. Interaction of lipid with phospho-N-acetylmuramylpentapeptide translocase

Weppner, William A.; Neuhaus, Francis C.

doi:10.1016/0005-2736(79)90186-x

Cited by 23 publications

(13 citation statements)

References 39 publications

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“…The presence of alternating hydrophobic and hydrophilic segments in its primary structure clearly suggested that MraY was an integral membrane protein spanning the cytoplasmic membrane several times (Ikeda et al, 1991). Moreover, a lipid microenvironment was shown to be required for the MraY activity Umbreit & Strominger, 1972a;Geis & Plapp, 1978;Weppner & Neuhaus, 1979). More recently, Bouhss et al (1999) determined the two-dimensional membrane topology of both the E. coli and S. aureus MraY translocases, using b-lactamase fusion experiments.…”

Section: Translocase I Reaction and Identification Of The Mray Genementioning

confidence: 99%

The biosynthesis of peptidoglycan lipid-linked intermediates

et al. 2008

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The biosynthesis of bacterial cell wall peptidoglycan is a complex process involving many different steps taking place in the cytoplasm (synthesis of the nucleotide precursors) and on the inner and outer sides of the cytoplasmic membrane (assembly and polymerization of the disaccharide-peptide monomer unit, respectively). This review summarizes the current knowledge on the membrane steps leading to the formation of the lipid II intermediate, i.e. the substrate of the polymerization reactions. It makes the point on past and recent data that have significantly contributed to the understanding of the biosynthesis of undecaprenyl phosphate, the carrier lipid required for the anchoring of the peptidoglycan hydrophilic units in the membrane, and to the characterization of the MraY and MurG enzymes which catalyze the successive transfers of the N-acetylmuramoyl-peptide and N-acetylglucosamine moieties onto the carrier lipid, respectively. Enzyme inhibitors and antibacterial compounds interfering with these essential metabolic steps and interesting targets are presented.

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Section: Translocase I Reaction and Identification Of The Mray Genementioning

confidence: 99%

The biosynthesis of peptidoglycan lipid-linked intermediates

et al. 2008

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“…Ratios significantly > 1 represent enrichment of a lipid in whole cells, whereas values significantly < 1 represent depletion in whole cells. are influenced by the surrounding lipid environment (Machtiger & Fox, 1973;Esfahani et al, 1977;Dancey & Shapiro, 1977;Weppner & Neuhaus, 1979). These points provide a framework for the remainder of the discussion.…”

Section: Lipid Composition Of Membranes From Whole Cells and Minicellsmentioning

confidence: 99%

Composition of Membranes from Whole Cells and Minicells of Bacillus subtilis

Shohayeb¹,

Chopra²

1985

Microbiology

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The composition of membranes from whole cells and minicells of Bacillus subtilis strain BD474 was examined. Two-dimensional electrophoresis showed that the content of several individual polypeptides differed in the two membrane types. Whole cell membranes appeared to contain more penicillin binding protein (PBP) 2a, glycerol-3-phosphate dehydrogenase, succinate dehydrogenase and NADH dehydrogenase than minicell membranes, but less PBP2b, lactate dehydrogenase and malate dehydrogenase. Glycerol-3-phosphate dehydrogenase and succinate dehydrogenase were unstable, but the other enzymes and PBPs were stable after inhibition of protein synthesis by chloramphenicol. Minicells synthesized peptidoglycan because they incorporated T-labelled acetylglucosamine into acid precipitable material. However, the rate of incorporation in minicells was only 5% of the value observed in whole cells. Whole cell and minicell membranes contained the same polar lipids and fatty acids, but the whole cell membranes were enriched in phosphatidylglycerol, diglycosyldiacylglycerol, iso-C , and anteiso-C, fatty acids, but depleted of phosphatidylethanolamine, iso-c,,, iso-c, 6, n-C, 6 and anteiso-C , fatty acids.Ahhrr ia f ion : P B P, pen i c i 11 in binding protein .

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“…Lipid composition is extensively regulated in E. coli in response to growth temperature. Acyl chain composition and polar head groups can alter the activities of membrane-bound enzymes (18,24,41). Our results indicate that no changes in the synthesis of these molecules occurred during the cell cycle, eliminating this as a possible mechanism for regulation.…”

Section: Discussionmentioning

confidence: 69%

“…Lipids are essential for the activities of many membrane-bound enzymes (10). Both the types and quantities of lipids can alter enzyme activity (10,17,18,24,41). Membrane lipids are highly regulated in bacterial systems (11,36).…”

mentioning

confidence: 99%

Lipid synthesis during the Escherichia coli cell cycle.

Carty¹,

Ingram²

1981

Journal of Bacteriology

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Lipid synthesis was examined in Escherichia coli cells at different stage of cell division. Exponentially growing cells were pulse-labeled with appropriate isotopes for 0.1 generation time, inactivated, and separated by size on a sucrose gradient. An abrupt increase in the rate of lipid synthesis occurred which was coincident with the initiation of cross walls. In contrast, the rate of protein synthesis during this same interval remained constant, resulting in an increased lipid/protein ratio in dividing cells. No changes in the composition of phospholipid head groups, fatty acids, or phospholipid molecular species were observed in cells at different stages of division. The observed increase in the rate of lipid synthesis may reflect a means by which the activities of membrane-associated enzymes are modulated during cross wall formation.

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Initial membrane reaction in peptidoglycan synthesis. Interaction of lipid with phospho-N-acetylmuramylpentapeptide translocase

Cited by 23 publications

References 39 publications

The biosynthesis of peptidoglycan lipid-linked intermediates

The biosynthesis of peptidoglycan lipid-linked intermediates

Composition of Membranes from Whole Cells and Minicells of Bacillus subtilis

Lipid synthesis during the Escherichia coli cell cycle.

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