Biological roles of two new murein hydrolases of Streptococcus pneumoniae representing examples of module shuffling

被引:30
作者
López, R [1 ]
González, MP [1 ]
García, E [1 ]
García, JL [1 ]
García, P [1 ]
机构
[1] CSIC, Ctr Invest Biol, Dept Mol Microbiol, E-28006 Madrid, Spain
关键词
Streptococcus pneumoniae; murein hydrolase; module shuffling;
D O I
10.1016/S0923-2508(00)00172-8
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
We have found two murein hydrolases (LytB and LytC) tightly bound to the cell envelope that have completely changed the domain building plan previously reported for the murein hydrolases of Streptococcus pneumoniae. The active center of LytB and LytC is located at the C-terminal, whereas the binding domain is at the N-terminal. LytC has been characterized as the first lysozyme of S. pneumoniae and behaves as an autolysin at 30 degrees C. LytB appears as the main hydrolase responsible for cell separation since inactivation of lytB leads to the formation of long chains of more than 100 cells. These findings indicate that genetic adaptation of mobile domains is extremely efficient in pneumococcus. (C) 2000 Editions scientifiques et medicales Elsevier SAS.
引用
收藏
页码:437 / 443
页数:7
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