The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains (research by P. García, M.P. González, J.L. García, R. López, Molecular Microbiology 1999, 22, 128).

MOLLERACH M

Chemtracts. Biochemistry and Molecular Biology

Springer

Año: 2000 vol. 13 p. 679 - 682

This paper represents an important advance in the knowledge of the lytic enzymes of S. pneumoniae. The enzyme reported here is the first muramidase characterized in this species . The authors used a genetical and a biochemical approach to study the role of this enzyme in the pneumococcal system and provided evidence on the participation in the autolysis developed upon incubation at 30°C. An interesting especulation was made about the relationship between this property and the in vivo transformation of chromosomal genes in pneumococcus. The exhaustive analysis of the the C-terminal moiety allowed them to determine that it behaves as a true domain. The authors demonstrated that it was able to acquire an active conformation when synthesized in E. coli, confirming the assumption that this part is the catalytic domain of the molecule. The observed change in the general building plan characteristic of choline binding proteins was wisely developed to make striking evolutionary considerations about the interchanges of modules in the pneumococcal system and the plasticity of the genes coding for proteins with a modular design.