Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 14, Pages 9463-9472Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R113.520015
Keywords
Bacterial Protein Kinases; Bacterial Signal Transduction; Signal Transduction; Signaling; Protein-tyrosine Kinase (Tyrosine Kinase); BY-kinases; Mycobacterium tuberculosis PtkA; Tyr Kinase
Categories
Funding
- Canadian Institutes of Health Research (CIHR) [MOP-106622]
Ask authors/readers for more resources
Microbial ester kinases identified in the past 3 decades came as a surprise, as protein phosphorylation on Ser, Thr, and Tyr amino acids was thought to be unique to eukaryotes. Current analysis of available microbial genomes reveals that eukaryote-like protein kinases are prevalent in prokaryotes and can converge in the same signaling pathway with the classical microbial two-component systems. Most microbial tyrosine kinases lack the eukaryotic Hanks domain signature and are designated tyrosine kinases based upon their biochemical activity. These include the tyrosine kinases termed bacterial tyrosine kinases (BY-kinases), which are responsible for the majority of known bacterial tyrosine phosphorylation events. Although termed generally as bacterial tyrosine kinases, BY-kinases can be considered as one family belonging to the superfamily of prokaryotic protein-tyrosine kinases in bacteria. Other members of this superfamily include atypical odd tyrosine kinases with diverse mechanisms of protein phosphorylation and the eukaryote-like Hanks-type tyrosine kinases. Here, we discuss the distribution, phylogeny, and function of the various prokaryotic protein-tyrosine kinases, focusing on the recently discovered Mycobacterium tuberculosis PtkA and its relationship with other members of this diverse family of proteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available