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STREPTOCOCCAL L FORMS V.

Acid-Soluble Nucleotides of a Group A Streptococcus and Derived L Form

^a Department of Biological Chemistry, University of Illinois College of Medicine, Chicago, Illinois
^b Research Laboratories, Department of Biochemistry, Albert Einstein Medical Center, Philadelphia, Pennsylvania

ABSTRACT

EDWARDS, JOHN (University of Illinois College of Medicine, Chicago, and Albert Einstein Medical Center, Philadelphia, Pa.) AND CHARLES PANOS. Streptococcal L-forms. V. Acid-soluble nucleotides of a group A Streptococcus and derived L form. J. Bacteriol. 84:1202–1208. 1962.—This report deals with a comparison of the acid-soluble nucleotides from a group A, type 12, ß-hemolytic streptococcus and a derived stable L form. This is the first report of the presence of a cell-wall precursor (uridine diphosphate-muramic acid-peptide) in a stable L form. Cells of each organism were obtained during their logarithmic phases of growth, harvested by centrifugation, and washed with osmotically protective NaCl solutions. The analytical procedures were essentially those of Franzen and Binkley. Calculated values indicated that these results could not be accounted for by dry-weight differences due to loss of the streptococcal cell wall. It was found that both organisms contained the same amount of total nucleotide material. The L form contained no uridine monophosphate (UMP), a large concentration of uridine diphosphate (UDP)-muramic acid-peptide, and a significant increase of UDP-N-acetylglucosamine. A similar nucleotide containing muramic acid-peptide was not demonstrable in the parent coccus. Instead, UMP and an unidentified uridine nucleotide were resolved in this region. Analyses of extracts from this streptococcal L form indicate the probable presence of two of the three nucleotides originally isolated by Park from penicillin-treated Staphylococcus aureus. The presence of the UDP-muramic acid-peptide cell-wall precursor in the L form cultured in the continual absence of penicillin points to an inability of this form to resynthesize the rigid cell wall and indicates that this synthetic mechanism has been permanently impaired.

¹ To be submitted in partial fulfillment for the degree of Doctor of Philosophy.

² Senior research fellow (SF 531), 1960. Present address: Research Laboratories, Department of Biochemistry, Albert Einstein Medical Center, Northern Division, Philadelphia, Pa.