Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis

被引:61
作者
Huard, C
Miranda, G
Wessner, FO
Bolotin, A
Hansen, J
Foster, SJ
Chapot-Chartier, MP
机构
[1] INRA, Unite Biochim & Struct Prot, F-78352 Jouy En Josas, France
[2] INRA, Unite Genet Microbienne, F-78352 Jouy En Josas, France
[3] Univ Sheffield, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England
来源
MICROBIOLOGY-SGM | 2003年 / 149卷
关键词
D O I
10.1099/mic.0.25875-0
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A gene encoding a putative peptidoglycan hydrolase, named acmB, which is a paralogue of the major autolysin acmA gene, was identified in the Lactococcus lactis genome sequence. The acmB gene is transcribed in L. lactis MG1363 and its expression is modulated during cellular growth. The encoded AcmB protein has a modular structure with three domains: an N-terminal domain, especially rich in Ser, Thr, Pro and Asn residues, resembling a cell-wall-associated domain; a central domain homologous to the Enterococcus hirae muramidase catalytic domain; and a C-terminal domain of unknown function. A recombinant AcmB derivative, devoid of its N-terminal domain, was expressed in Escherichia coli. It exhibited hydrolysing activity on the peptidoglycan of several Gram-positive bacteria, including L. lactis. Though showing sequence similarity with enterococcal muramidase, AcmB has N-acetylglucosaminidase specificity. The acmB gene was inactivated in order to evaluate the role of the enzyme. AcmB does not appear to be involved in cell separation but contributes to cellular autolysis.
引用
收藏
页码:695 / 705
页数:11
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