Bacterial FHA domains: neglected players in the phospho-threonine signalling game?
Forkhead-associated (FHA) domains bind phospho-threonine peptides and are known to mediate phosphorylation-dependent protein-protein interactions in a variety of eukaryotic settings. However, their role in bacterial physiology and signalling has been largely neglected. We have surveyed bacterial FHA domains and discovered that they are implicated in many bacterial processes, including regulation of cell shape, type III secretion, sporulation, pathogenic and symbiotic host-bacterium interactions, carbohydrate storage and transport, signal transduction and ethambutol resistance. The way is now open to identify the targets of each FHA domain, and their roles in cellular physiology, and perhaps even to develop novel FHA-blocking antibacterial agents.
Pallen
Mark
M
Division of Immunity & Infection, Birmingham University Medical School, UK. m.pallen@bham.ac.uk
Chaudhuri
Roy
R
Khan
Arshad
A
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D051858:Forkhead Transcription Factors; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism; D010769:Phosphothreonine / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D015398:Signal Transduction; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D051858:Forkhead Transcription Factors; D009687:Nuclear Proteins; D014157:Transcription Factors; D010769:Phosphothreonine