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Identification of Mur, an atypical peptidoglycan hydrolase derived from Leuconostoc citreum

Cibik, R., Tailliez, P., Langella, P., Chapot-Chartier, M.P.
Applied and environmental microbiology 2001 v.67 no.2 pp. 858-864
Leuconostoc, O-glycoside hydrolases, genes, nucleotide sequences, amino acid sequences, enzyme activity, hydrolysis, recombinant proteins, Lactococcus lactis, bacterial proteins
A gene encoding a protein homologous to known bacterial N-acetyl-muramidases has been cloned from Leuconostoc citreum by a PCR-based approach. The encoded protein, Mur, consists of 209 amino acid residues with a calculated molecular mass of 23,821 Da including a 31-amino-acid putative signal peptide. In contrast to most of the other known peptidoglycan hydrolases, L. citreum Mur protein does not contain amino acid repeats involved in cell wall binding. The purified L. citreum Mur protein was shown to exhibit peptidoglycan-hydrolyzing activity by renaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. An active chimeric protein was constructed by fusion of L. citreum Mur to the C-terminal repeat-containing domain (cA) of AcmA, the major autolysin of Lactococcus lactis. Expression of the Mur-cA fusion protein was able to complement an acmA mutation in L. lactis; normal cell separation after cell division was restored by Mur-cA expression.