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Gene. 1990 Apr 30;89(1):69-75.

Cloning and expression of gene fragments encoding the choline-binding domain of pneumococcal murein hydrolases.

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Centro de Investigaciones Biológicas, C.S.I.C., Velázquez, Madrid, Spain.


The cloning in Escherichia coli of the 3' moieties of the lytA and cpl-1 genes is described, coding for the C-terminal regions of the lytic amidase of Streptococcus pneumoniae and the phage Cp-1 lysozyme, respectively. The truncated genes were overexpressed in E. coli and the purified polypeptides showed a great affinity for choline, although they were devoid of cell wall-degrading activity. Biochemical and circular dichroism analyses indicated that these are the domains responsible for the specific recognition of the choline-containing pneumococcal cell walls by the lytic enzymes. The data presented here suggested that these choline-binding domains can function independently of their catalytic domains.

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