Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis.
A cascade of protein phosphorylation, initiated by autophosphorylation of the CheA protein, may be important in the signal transduction pathway of bacterial chemotaxis. A proteolytic fragment of CheA cannot autophosphorylate, but can still transfer phosphate to proteins that generate excitation and adaptation signals. The site of CheA phosphorylation is His 48; mutants altered at this position are non-chemotactic. Similar mechanisms of transient protein phosphorylation and phosphoryl group transfer seem to be involved in processing sensory data and in activating specific gene expression.
Hess
J F
JF
Division of Biology, California Institute of Technology, Pasadena 91125.
Bourret
R B
RB
Simon
M I
MI
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D002633:Chemotaxis; D002851:Chromatography, High Pressure Liquid; D006639:Histidine / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D009154:Mutation; D010710:Phosphates / Q000378:metabolism*; D010766:Phosphorylation; D015398:Signal Transduction
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D010710:Phosphates; D006639:Histidine