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Isolation and Characterization of Mutants of the Bacillus subtilis Oligopeptide Permease with Altered Specificity of Oligopeptide Transport

Jonathan Solomon, Laura Su, Stanley Shyn, and Alan D. Grossman^*

Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Received 2 July 2003/ Accepted 8 August 2003

Bacterial oligopeptide permeases are members of the large family of ATP binding cassette transporters and typically import peptides of 3 to 5 amino acids, apparently independently of sequence. Oligopeptide permeases are needed for bacteria to utilize peptides as nutrient sources and are sometimes involved in signal transduction pathways. The Bacillus subtilis oligopeptide permease stimulates competence development and the initiation of sporulation, at least in part, by importing specific signaling peptides. We isolated rare, partly functional mutations in B. subtilis opp. The mutants were resistant to a toxic tripeptide but still retained the ability to sporulate and/or become competent. The mutations, mostly in the oligopeptide binding protein located on the cell surface, affected residues whose alteration appears to change the specificity of oligopeptide transport.

Present address: Elixir Pharmaceuticals, Cambridge, MA 02139.

Present address: Department of Internal Medicine, Stanford Hospital and Clinic, Stanford, CA 94305.

Present address: Division of Biological Sciences, University of California at San Diego, La Jolla, CA 92093.

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