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Biosynthetic reactions forming crosslinked peptidoglycan in Escherichia coli in which the step of crosslinkage formation is very sensitive to cephalexin and penicillin G could be demon strated in a membrane preparation of E. coll. The cells of E. coli strain which lack activities of penicillin-binding protein (PBP)-1Bs1) and overproduce PBP-3 (about 10 times control) were used as the source of the membrane preparation. It was prepared by introducing colEl plasmid pLC 26-62) into the mrc (PBP1Bs-) strain JST975srev6.1) The plasmid pLC 26-6 from the plasmid bank of Clarke and Carbon" has been reported to involve a chro mosomal part covering from leuA to ftsI,3) the structure gene of PBP-3.4) The cells at the late log phase of growth in a rich medium containing colicin El were gently sonicated in 0.05M Tris-HCl buffer, pH 7.6, and the mem brane fraction was obtained as described pre viously.1) The membrane fraction showed ac tivity of synthesizing peptidoglycan from its nucleotide precursors, UDP-MurNAc-penta peptide (L-Ala-D-Glu-m-[14C]A2pm-D-Ala-DAla) and UDP-GlcNAc under reaction con ditions described previously1) with slight modi fications (Table I). About 1.5-3 times as much [14C]-peptidoglycan was formed by the membrane preparations from cells overproduc ing PBP-3 as that by membrane preparations from the control PBP-1Bscells producing a normal amount of PBP-3 (data not shown). The formed peptidoglycan was digested with lysozyme and the degree of crosslinking was measured as previously described.1) It was crosslinked to 6-10% (Table I), which is considerably lower than the crosslinkage of the peptidoglycan formed by pure PBP-lBs

agricultural and biological chemistry

In vitro peptidoglycan synthesis which is very sensitive to cephalexin and penicillin G in Escherichia coli: Presumable septum-forming reaction sequence.