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Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands
- Source :
- eLife, Vol 6 (2017), eLife
- Publication Year :
- 2017
- Publisher :
- eLife Sciences Publications Ltd, 2017.
-
Abstract
- Staphylococcus aureus pathogenicity islands (SaPIs), such as SaPI1, exploit specific helper bacteriophages, like 80α, for their high frequency mobilization, a process termed ‘molecular piracy’. SaPI1 redirects the helper’s assembly pathway to form small capsids that can only accommodate the smaller SaPI1 genome, but not a complete phage genome. SaPI1 encodes two proteins, CpmA and CpmB, that are responsible for this size redirection. We have determined the structures of the 80α and SaPI1 procapsids to near-atomic resolution by cryo-electron microscopy, and show that CpmB competes with the 80α scaffolding protein (SP) for a binding site on the capsid protein (CP), and works by altering the angle between capsomers. We probed these interactions genetically and identified second-site suppressors of lethal mutations in SP. Our structures show, for the first time, the detailed interactions between SP and CP in a bacteriophage, providing unique insights into macromolecular assembly processes.
- Subjects :
- 0301 basic medicine
Scaffold protein
Staphylococcus aureus
Genomic Islands
QH301-705.5
Structural Biology and Molecular Biophysics
Science
030106 microbiology
S. aureus pathogenicity island 1 (SaPI1)
cryo-electron microscopy
bacteriophage 80alpha
Genome
General Biochemistry, Genetics and Molecular Biology
Microbiology
Bacteriophage
Viral Proteins
03 medical and health sciences
Capsid
Bacterial Proteins
Protein Interaction Mapping
Bacteriophages
Biology (General)
Microbiology and Infectious Disease
General Immunology and Microbiology
biology
three-dimensional reconstruction
Virus Assembly
General Neuroscience
Cryoelectron Microscopy
Capsomere
virus structure and assembly
General Medicine
biology.organism_classification
Pathogenicity island
Cell biology
Macromolecular assembly
030104 developmental biology
Structural biology
Medicine
Other
Research Article
Subjects
Details
- Language :
- English
- Volume :
- 6
- Database :
- OpenAIRE
- Journal :
- eLife
- Accession number :
- edsair.doi.dedup.....40fb84e320e57c2e74ceafa7e5fa81aa