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Mol Microbiol. 1994 Aug;13(3):417-26.

Identification of a second oligopeptide transport system in Bacillus subtilis and determination of its role in sporulation.

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Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, California 92037.


Sporulation in Bacillus subtilis depends on an intact oligopeptide transport system, the Opp system. Mutants in opp sporulate poorly but second-site revertants can be found that restore sporulation and peptide transport. These second-site mutations were found in a second oligopeptide transport system, app, in which the peptide-binding protein, AppA, is mutant owing to a frame-shift mutation, and the revertants restore the original frame. The AppA mutation is present in the 168 strain of B. subtilis. The app operon consists of five genes in the order appD-appF-appA-appB-appC, with the locus designations corresponding to their homologue in the opp operon. Homology between the app and opp proteins ranges from 54% identity for AppF and OppF, to 22% identity for AppA and OppA. Both the App and Opp permease systems can transport tetra- and pentapeptides, but tripeptides are not transported by the App system. Strains of the genotype app+ opp- are resistant to the tripeptide antibiotic bialaphos. The repaired App system can substitute completely for the Opp system in both sporulation and competence for genetic transformation. The phenotypes raised some speculation about the subunit configuration of the Opp system.

[Indexed for MEDLINE]

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