Evidence for a coiled-coil interaction mode of disordered proteins from bacterial type III secretion systems.
Gene clusters encoding various type III secretion system (T3SS) injectisomes, frequently code downstream of the conserved atpase gene for small hydrophilic proteins whose amino acid sequences display a propensity for intrinsic disorder and coiled-coil formation. These properties were confirmed experimentally for a member of this class, the HrpO protein from the T3SS of Pseudomonas syringae pv phaseolicola: HrpO exhibits high alpha-helical content with coiled-coil characteristics, strikingly low melting temperature, structural properties that are typical for disordered proteins, and a pronounced self-association propensity, most likely via coiled-coil interactions, resulting in heterogeneous populations of quaternary complexes. HrpO interacts in vivo with HrpE, a T3SS protein for which coiled-coil formation is also strongly predicted. Evidence from HrpO analogues from all T3SS families and the flagellum suggests that the extreme flexibility and propensity for coiled-coil interactions of this diverse class of small, intrinsically disordered proteins, whose structures may alter as they bind to their cognate folded protein targets, might be important elements in the establishment of protein-protein interaction networks required for T3SS function.
Institute of Molecular Biology & Biotechnology, Foundation of Research & Technology, Vasilika Vouton, Heraklion, Crete, Greece.
Anastasia D
AD
Gazi
Marina
M
Bastaki
Spyridoula N
SN
Charova
Eirini A
EA
Gkougkoulia
Efthymios A
EA
Kapellios
Nicholas J
NJ
Panopoulos
Michael
M
Kokkinidis
D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000378:metabolism; D005407:Flagella / Q000737:chemistry; D008954:Models, Biological; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D044224:Pseudomonas syringae / Q000378:metabolism; D013696:Temperature; D020798:Two-Hybrid System Techniques
D001426:Bacterial Proteins; D002352:Carrier Proteins