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Processing, assembly and localization of a Bacillus anthracis spore protein
K L Moody1, A Driks2, G L Rother1
1Bacteriology Division, US Army Medical Research Institute of Infectious Diseases, 1425 Porter Street, Fort Detrick, MD 21702, USA.
Microbiology (Reading, England)
|October 17, 2009
Summary
Bacillus anthracis spore coat protein BxpA undergoes unexpected processing. Mutations in Tgl and YabG proteins alter BxpA
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- Bacillus spores possess protective macromolecular shells, including the coat.
- The Bacillus anthracis spore coat is crucial for anthrax pathogenesis.
- BxpA is a protein component of Bacillus spore outer layers.
Purpose of the Study:
- To analyze the location and processing of Bacillus anthracis spore protein BxpA.
- To investigate the role of spore proteins Tgl and YabG in BxpA maturation.
Main Methods:
- Analysis of BxpA location using SDS-PAGE.
- Generation of yabG and tgl gene mutations in Bacillus anthracis strains.
- Assessment of BxpA assembly and apparent mass in mutant strains.
Main Results:
- BxpA is located below the spore coat, associated with the cortex.
- BxpA exhibits significantly lower apparent mass than predicted, suggesting post-translational modification.
- Mutations in tgl and yabG genes result in increased apparent mass of BxpA.
- Tgl appears to cross-link BxpA, while YabG's role in proteolysis is more complex than anticipated.
Conclusions:
- BxpA undergoes significant post-translational processing, including cross-linking by Tgl and proteolysis by YabG.
- These findings reveal novel insights into Bacillus spore protein maturation.
- Proteolysis and cross-linking may be common mechanisms in Bacillus spore assembly.
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