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Incorporation of D-Alanine into the Membrane of Streptococcus pyogenes and Its Stabilized L-Form

¹ Department of Microbiology, Jefferson Medical College of Thomas Jefferson University, Philadelphia, Pennsylvania 19107, and the Biochemistry Division, Department of Chemistry, Northwestern University, Evanston, Illinois 60201

ABSTRACT

A principal aim of this study was to explain our earlier finding of a lack of D-alanine in the glycerol teichoic acid from the membrane of a stabilized L-form of Streptococcus pyogenes (B. M. Slabyj and C. Panos, 1973. J. Bacteriol. 114:934-942). It was found that the incorporation of D-alanine into the membrane teichoic acid of S. pyogenes requires either supernatant fraction or two enzymes from supernatant fraction, stimulator (D-alanine activating enzyme) and D-alanine:membrane acceptor ligase, plus membrane fragments, ATP and Mg²⁺. A similar system from the L-form is inoperative. Also, no incorporation is observed with L-form or coccal supernatant fractions when L-form membranes are used. However, D-alanine incorporation is observed when L-form enzymes are used with membrane fragments from the parental streptococcus. Thus, the L-form possesses the required soluble components for D-alanine incorporation but the L-form membrane cannot function as acceptor even though it contains D-alanine-deficient membrane teichoic acid. These results suggest that a defect has occurred in the membrane of this stabilized L-form for D-alanine incorporation into membrane teichoic acid.

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