PMID: 108266May 25, 1979

Dissociation and reconstitution of membranes synthesizing the peptidoglycan of Bacillus megaterium. A protein factor for the polymerization step.

The Journal of Biological Chemistry
A Taku, D P Fan

Abstract

Cholate-solubilized Bacillus megaterium membranes can be reconstituted by dialysis in the presence of magnesium ion to regain approximately 12% of the original peptidoglycan synthetic activity. Bio-Gel A-5m filtration of the solubilized components shows that all of the compounds necessary for peptidoglycan synthesis can be dissociated into material with a molecular weight of less than approximately 68,000. Using this reconstitution system, an assay has been developed for a new protein factor, PG-II, of B. megaterium. This factor could be combined with phospho-N-acetylmuramyl pentapeptide translocase and N-acetylglucosaminyl transferase to synthesize polymerized peptidoglycan from the precursors UDP-N-acetylmuramyl pentapeptide and UDP-N-acetylglucosamine. In the absence of PG-II, the disaccharide pentapeptide substrate for the polymerase was accumulated. In the presence of this factor, the amount of the substrate was diminished and polymeric peptidoglycan was formed. Therefore, PG-II was likely to be necessary for the polymerization step and may well have been the polymerase itself. From three chromatographic steps developed for the purification of PG-II, it seemed likely that a single protein with a molecular weight of approxi...Continue Reading

Related Concepts

Bacillus megaterium
Plasma Membrane
Cholic Acids
Magnesium
Pseudomurein
Protoplasts

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