A PilZ domain protein for chemotaxis adds another layer to c-di-GMP-mediated regulation of flagellar motility.
Cyclic diguanylate monophosphate (c-di-GMP) is a ubiquitous second messenger in bacteria. In this issue of Science Signaling, Xu et al show that c-di-GMP regulates chemotaxis by binding to the PilZ domain protein MapZ to alter the methyltransferase activity of its protein partner CheR, fleshing out the c-di-GMP signaling network of the opportunistic pathogen Pseudomonas aeruginosa.
Department of Cell Biology and Molecular Genetics and Maryland Pathogen Research Institute, University of Maryland, College Park, College Park, MD 20742, USA.
Mona W
MW
Orr
Department of Cell Biology and Molecular Genetics and Maryland Pathogen Research Institute, University of Maryland, College Park, College Park, MD 20742, USA. vtlee@umd.edu.
Vincent T
VT
Lee
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002633:Chemotaxis / Q000502:physiology*; D006152:Cyclic GMP / Q000031:analogs & derivatives* / Q000235:genetics / Q000378:metabolism; D005407:Flagella / Q000235:genetics / Q000378:metabolism*; D009068:Movement / Q000502:physiology*; D011550:Pseudomonas aeruginosa / Q000235:genetics / Q000378:metabolism*; D015290:Second Messenger Systems / Q000502:physiology*
D001426:Bacterial Proteins; C062025:bis(3',5')-cyclic diguanylic acid; D006152:Cyclic GMP