Identification of a malate chemoreceptor in Pseudomonas aeruginosa by screening for chemotaxis defects in an energy taxis-deficient mutant.
We found that a robust energy taxis response mediated by the Aer receptor can sometimes mask chemotaxis mediated by other methyl-accepting chemotaxis proteins (MCPs) in Pseudomonas aeruginosa. We identified PA2652 as a chemoreceptor for malate by screening aer mcp double mutants by using swarm plate assays.
Alvarez-Ortega
Carolina
C
Department of Microbiology, Box 357242, 1705 N.E. Pacific Street, University of Washington, Seattle, WA 98195-7242, USA.
Harwood
Caroline S
CS
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D002628:Chemoreceptor Cells / Q000378:metabolism*; D002633:Chemotaxis / Q000235:genetics / Q000502:physiology*; D008293:Malates / Q000378:metabolism*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D000072236:Methyl-Accepting Chemotaxis Proteins; D009154:Mutation; D011550:Pseudomonas aeruginosa / Q000235:genetics* / Q000378:metabolism / Q000502:physiology
D001426:Bacterial Proteins; D008293:Malates; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C030298:malic acid