Bacterial tyrosine kinases: evolution, biological function and structural insights
C Grangeasse, S Nessler… - … Transactions of the …, 2012 - royalsocietypublishing.org
Reversible protein phosphorylation is a major mechanism in the regulation of fundamental
signalling events in all living organisms. Bacteria have been shown to possess a versatile …
signalling events in all living organisms. Bacteria have been shown to possess a versatile …
Tyrosine-kinases in bacteria: from a matter of controversy to the status of key regulatory enzymes
E Bechet, S Guiral, S Torres, I Mijakovic, AJ Cozzone… - Amino Acids, 2009 - Springer
When considering protein phosphorylation in bacteria, phosphorylation of aspartic acid and
histidine residues mediated by the two-component systems is the first to spring to mind. And …
histidine residues mediated by the two-component systems is the first to spring to mind. And …
Microbial protein-tyrosine kinases
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 …
phosphorylation on Ser, Thr, and Tyr amino acids was thought to be unique to eukaryotes …
Bacterial tyrosine-kinases: Structure–function analysis and therapeutic potential
Since the characterization of genes encoding Ser/Thr-kinases and Tyr-kinases in bacteria, in
1991 and 1997, respectively, a growing body of evidence has been reported showing the …
1991 and 1997, respectively, a growing body of evidence has been reported showing the …
Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology
C Grangeasse, AJ Cozzone, J Deutscher… - Trends in biochemical …, 2007 - cell.com
Tyrosine phosphorylation is a key device in numerous cellular functions in eukaryotes, but in
bacteria this protein modification was largely ignored until the mid-1990s. The first …
bacteria this protein modification was largely ignored until the mid-1990s. The first …
Evolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substrates
It has often been speculated that bacterial protein-tyrosine kinases (BY-kinases) evolve
rapidly and maintain relaxed substrate specificity to quickly adopt new substrates when …
rapidly and maintain relaxed substrate specificity to quickly adopt new substrates when …
Tyrosine phosphorylation as a widespread regulatory mechanism in prokaryotes
Phosphorylation events modify bacterial and archaeal proteomes, imparting cells with rapid
and reversible responses to specific environmental stimuli or niches. Phosphorylated …
and reversible responses to specific environmental stimuli or niches. Phosphorylated …
Characterization of a bacterial gene encoding an autophosphorylating protein tyrosine kinase
C Grangeasse, P Doublet, E Vaganay, C Vincent… - Gene, 1997 - Elsevier
Acinetobacter johnsonii harbors a protein tyrosine kinase activity that is able to catalyze
autophosphorylation, like a number of eukaryotic tyrosine kinases. A biochemical and …
autophosphorylation, like a number of eukaryotic tyrosine kinases. A biochemical and …
Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues
Bacteria possess protein serine/threonine and tyrosine kinases which resemble eukaryal
kinases in their capacity to phosphorylate multiple substrates. We hypothesized that the …
kinases in their capacity to phosphorylate multiple substrates. We hypothesized that the …
Protein-serine/threonine/tyrosine kinases in bacterial signaling and regulation
In this review, we address some recent developments in the field of bacterial protein
phosphorylation, focusing specifically on serine/threonine and tyrosine kinases. We present …
phosphorylation, focusing specifically on serine/threonine and tyrosine kinases. We present …