title: Molecular architecture of the "stressosome," a signal integration and transduction hub.
abstract: A commonly used strategy by microorganisms to survive multiple stresses involves a signal transduction cascade that increases the expression of stress-responsive genes. Stress signals can be integrated by a multiprotein signaling hub that responds to various signals to effect a single outcome. We obtained a medium-resolution cryo-electron microscopy reconstruction of the 1.8-megadalton "stressosome" from Bacillus subtilis. Fitting known crystal structures of components into this reconstruction gave a pseudoatomic structure, which had a virus capsid-like core with sensory extensions. We suggest that the different sensory extensions respond to different signals, whereas the conserved domains in the core integrate the varied signals. The architecture of the stressosome provides the potential for cooperativity, suggesting that the response could be tuned dependent on the magnitude of chemophysical insult.
authors.affiliation: Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle-upon-Tyne NE2 4HH, UK.
authors.forename: Jon
authors.initials: J
authors.lastname: Marles-Wright
authors.forename: Tim
authors.initials: T
authors.lastname: Grant
authors.forename: Olivier
authors.initials: O
authors.lastname: Delumeau
authors.forename: Gijs
authors.initials: G
authors.lastname: van Duinen
authors.forename: Susan J
authors.initials: SJ
authors.lastname: Firbank
authors.forename: Peter J
authors.initials: PJ
authors.lastname: Lewis
authors.forename: James W
authors.initials: JW
authors.lastname: Murray
authors.forename: Joseph A
authors.initials: JA
authors.lastname: Newman
authors.forename: Maureen B
authors.initials: MB
authors.lastname: Quin
authors.forename: Paul R
authors.initials: PR
authors.lastname: Race
authors.forename: Alexis
authors.initials: A
authors.lastname: Rohou
authors.forename: Willem
authors.initials: W
authors.lastname: Tichelaar
authors.forename: Marin
authors.initials: M
authors.lastname: van Heel
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Lewis
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D007091:Image Processing, Computer-Assisted; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012808:Sigma Factor / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D046912:Multiprotein Complexes; D010750:Phosphoproteins; C119218:RsbR protein, Bacillus subtilis; D012808:Sigma Factor; C119219:RsbT protein, Bacillus subtilis; D017346:Protein Serine-Threonine Kinases