Published online 20 March 2006
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Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine
Microbial Physiology and Genetics group, BioCentrum, Technical University of Denmark DK-2800 Lyngby, Denmark 1 Center for Experimental Bioinformatics, Department of Biochemistry and Molecular Biology, University of Southern Denmark DK-5230 Odense M, Denmark 2 Department of Molecular Biology, Rudjer Boskovic Institute 10002 Zagreb, Croatia 3 Department of Microbiology and Immunology, University of British Columbia Vancouver, British Columbia, V6T 1Z3, Canada
*To whom correspondence should be addresed. Tel: +385 14 57 12 58; Fax: +385 14 56 91 77; Email: vujaklij{at}irb.hr
Received November 19, 2005. Revised January 31, 2006. Accepted January 31, 2006.
Single-stranded DNA-binding proteins (SSBs) are required for repair, recombination and replication in all organisms. Eukaryotic SSBs are regulated by phosphorylation on serine and threonine residues. To our knowledge, phosphorylation of SSBs in bacteria has not been reported. A systematic search for phosphotyrosine-containing proteins in Streptomyces griseus by immunoaffinity chromatography identified bacterial SSBs as a novel target of bacterial tyrosine kinases. Since genes encoding protein-tyrosine kinases (PTKs) have not been recognized in streptomycetes, and SSBs from Streptomyces coelicolor (ScSSB) and Bacillus subtilis (BsSSB) share 38.7% identity, we used a B.subtilis protein-tyrosine kinase YwqD to phosphorylate two cognate SSBs (BsSSB and YwpH) in vitro. We demonstrate that in vivo phosphorylation of B.subtilis SSB occurs on tyrosine residue 82, and this reaction is affected antagonistically by kinase YwqD and phosphatase YwqE. Phosphorylation of B.subtilis SSB increased binding almost 200-fold to single-stranded DNA in vitro. Tyrosine phosphorylation of B.subtilis, S.coelicolor and Escherichia coli SSBs occured while they were expressed in E.coli, indicating that tyrosine phosphorylation of SSBs is a conserved process of post-translational modification in taxonomically distant bacteria.
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