1887

Abstract

The gene (renamed ) of IL1403 was shown to encode a peptidoglycan -acetylglucosamine deacetylase. Inactivation of in led to fully acetylated peptidoglycan, whereas cloning of on a multicopy plasmid vector resulted in an increased degree of peptidoglycan deacetylation, as shown by analysis of peptidoglycan constituent muropeptides. An increased amount of -unsubstituted glucosamine residues in peptidoglycan resulted in a reduction of the rate of autolysis of cells. The activity of the major autolysin AcmA was tested on cells or peptidoglycan with different degrees of de--acetylation. Deacetylated peptidoglycan exhibited decreased susceptibility to AcmA hydrolysis. This reduced susceptibility to AcmA did not result from reduced AcmA binding to peptidoglycan with an increasing degree of de--acetylation. In conclusion, enzymic -acetylglucosamine deacetylation protects peptidoglycan from hydrolysis by the major autolysin AcmA in cells, and this leads to decreased cellular autolysis.

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2007-10-01
2020-03-29
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