Authors: Alain J Cozzone Christophe Grangeasse Patricia Doublet Bertrand Duclos
Publish Date: 2004/01/24
Volume: 181, Issue: 3, Pages: 171-181
Abstract
Protein phosphorylation on tyrosine has been demonstrated to occur in a wide array of bacterial species and appears to be ubiquitous among prokaryotes This covalent modification is catalyzed by autophosphorylating ATPdependent proteintyrosine kinases that exhibit structural and functional features similar but not identical to those of their eukaryotic counterparts The reversibility of the reaction is effected by two main classes of proteintyrosine phosphatases one includes conventional eukaryoticlike phosphatases and dualspecific phosphatases and the other comprises acidic phosphatases of low molecular weight Less frequently a third class concerns enzymes of the polymerasehistidinol phosphatase type In terms of genomic organization the genes encoding a proteintyrosine phosphatase and a proteintyrosine kinase in a bacterial species are most often located next to each other on the chromosome In addition these genes are generally part of large operons that direct the coordinate synthesis of proteins involved in the production or regulation of exopolysaccharides and capsular polysaccharides Recent data provide evidence that there exists a direct relationship between the reversible phosphorylation of proteins on tyrosine and the production of these polysaccharidic polymers which are also known to be important virulence factors Therefore a new concept has emerged suggesting the existence of a biological link between proteintyrosine phosphorylation and bacterial pathogenicity
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