Summary: Three heat-sensitive mutants of 168, which lysed at the non-permissive temperature, have been shown under these conditions to be defective in the synthesis of peptidoglycan. This was caused by lesions in three different stages of peptidoglycan synthesis. In one mutant (), -alanine: -alanine ligase was defective, leading to the accumulation of UDP-MurAc--Ala--Glu--Apm; the mutation was closely linked (87% cotransducible) with , specifying alanine racemase. In a second mutant (), the lesion was in -acetyl--diaminopimelate deacylase, resulting in UDP-MurAc--Ala--Glu being accumulated, whilst in a third mutant (), UDP-MurAc--Ala--Glu--Apm--Ala--Ala was the peptidoglycan precursor accumulated although the enzyme defect has not been ascertained. Both and were located between and (AD), dapE being 25% cotransducible with (), whilst was 60 to 70% cotransducible with ().


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