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- Title
AcmA ofLactococcus lactisis anN-acetylglucosaminidase with an optimal number of LysM domains for proper functioning.
- Authors
Steen, Anton; Buist, Girbe; Horsburgh, Gavin J.; Venema, Gerard; Kuipers, Oscar P.; Foster, Simon J.; Kok, Jan
- Abstract
AcmA, the major autolysin ofLactococcus lactisMG1363 is a modular protein consisting of an N-terminal active site domain and a C-terminal peptidoglycan-binding domain. The active site domain is homologous to that of muramidase-2 ofEnterococcus hirae, however, RP-HPLC analysis of muropeptides released fromBacillus subtilispeptidoglycan, after digestion with AcmA, shows that AcmA is anN-acetylglucosaminidase. In the C-terminus of AcmA three highly similar repeated regions of 45 amino acid residues are present, which are separated by short nonhomologous sequences. The repeats of AcmA, which belong to the lysine motif (LysM) domain family, were consecutively deleted, removed, or, alternatively, one additional repeat was added, without destroying the cell wall-hydrolyzing activity of the enzymein vitro, although AcmA activity was reduced in all cases.In vivo, proteins containing no or only one repeat did not give rise to autolysis of lactococcal cells, whereas separation of the producer cells from the chains was incomplete. Exogenously added AcmA deletion derivatives carrying two repeats or four repeats bound to lactococcal cells, whereas the derivative with no or one repeat did not. In conclusion, these results show that AcmA needs three LysM domains for optimal peptidoglycan binding and biological functioning.
- Subjects
LACTOCOCCUS lactis; AUTOLYSIS; GLYCOASPARAGINASE; ANTIGEN-antibody reactions; BACILLUS subtilis; BACILLUS (Bacteria); GENETICS
- Publication
FEBS Journal, 2005, Vol 272, Issue 11, p2854
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2005.04706.x