Abstract
The external polysaccharide is a major component of Micrococcus lysodeikticus cell wall and displays distinct composition. The complete structure of the external polysaccharide had been elucidated as a basis for investigation of the cell wall structure-function relation. However, the mode of attachment of the polysaccharide to the peptidoglycan through a phosphodiester was not clear due to limitations in structural and biosynthetic studies. The present study describes purification of a lysozyme-resistant nondialyzable high-molecular-weight fragment of cell wall and identifies the sugar, D-glucose, as the point of external polysaccharide attachment to the peptidoglycan through a phosphate diester. Kinetic studies for the acid-catalyzed release of external polysaccharide from the peptidoglycan were performed in parallel with synthetic [methyl-2-acetamido-3-O-(D-1-carboxyethyl)-2-deoxy-alpha-D- glucopyranoside-6-yl]-alpha-D-glucopyranosyl phosphate and alpha-D-glucopyranosyl phosphate and showed the presence of a phosphodiester linkage between external polysaccharide and peptidoglycan. In addition, type of phosphate residue and cross-linking between muramic acid and protein part have been determined.
Highlights
The external polysaccharide is a major component of diester linkage involving some of the muramic acid residues
Shown that tunicamycin and bacitracin both inhibited the biosynthesis of external polysaccharide (11).In more recent studies, there is a good deal of evidence to suggest that a lipid intermediate containing glucose may be involved
The peptidoglycan moiety has been shown to include polysaccharide to the peptidoglycan, synthetic and commerpolysaccharide chains composed of alternate N-acetylglucos- cially available model compounds were utilized to define opamine andN-acetylmuramic acid units linked p(1-4) (2), timal conditions for the acid-catalyzed release of polysacchasimilar to those of numerous other peptidoglycans bound to ride from the peptidoglycan
Summary
It has been suggested that they are linked to the peptidoglycan moiety through a phosphate. Fractionation and Properties of Nondiulyzable Fraction CPCA.2-The nondiffusible cell wall was fractionated by ce-. This is publication 983 of the Lovett Memorial Group for the Study Tables I to IV, and Figs. 1 to 6) are presented in miniprint at theend of Disease Causing Deformities, Harvard Medical School and Mas- of this paper. Miniprint is read with the aid of a standard sachusetts General Hospital. The costs of publication of this article magnifying glass. Full size photocopies are available from the Journal were defrayed in part by the payment of page charges. This article of Biological Chemistry, 9650 Rockville Pike, Bethesda, MD 20814.
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