Identification of Mur, an atypical peptidoglycan hydrolase derived from Leuconostoc citreum
Identification of Mur, an atypical peptidoglycan hydrolase derived from Leuconostoc citreum
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DOI：
10.1128/aem.67.2.858-864.2001
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发表时间：
2001-02-01
影响因子：
4.4
通讯作者：
Chapot-Chartier, MP
中科院分区：
文献类型：
--
作者：
Cibik, R;Tailliez, P;Chapot-Chartier, MP
已通过基于PCR的方法从柠檬明串珠菌（Leuconostoc citreum）中克隆了编码与已知细菌N-乙酰胞壁酰胺酶同源的蛋白质的基因。编码的蛋白质Mur由209个氨基酸残基组成，计算分子量为23，821 Da，包括31个氨基酸的推定信号肽。与大多数已知的肽聚糖水解酶相比，L. CitreumMur蛋白不含参与细胞壁结合的氨基酸重复序列。纯化的L.通过复性十二烷基硫酸钠-聚丙烯酰胺凝胶电泳，柠檬酸Mur蛋白显示出肽聚糖水解活性。通过融合构建了具有活性的嵌合蛋白。citreum Mur与AcmA的C-末端含重复结构域（cA）连接，AcmA是乳酸乳球菌的主要自溶素。Mur-cA融合蛋白的表达能够补充L.乳酸菌;通过Mur-cA表达恢复细胞分裂后的正常细胞分离。
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 oft. 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.