title: The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation.
abstract: Bacillus subtilis spo0K mutants are blocked at the first step in sporulation. The spo0K strain was found to contain two mutations: one was linked to the trpS locus, and the other was elsewhere on the chromosome. The mutation linked to trpS was responsible for the sporulation defect (spo-). The unlinked mutation enhanced this sporulation deficiency but had no phenotype on its own. The spo- mutation was located in an operon of five genes highly homologous to the oligopeptide transport (Opp) system of Gram-negative species. Studies with toxic peptide analogues showed that this operon does indeed encode a peptide-transport system. However, unlike the Opp system of Salmonella typhimurium, one of the two ATP-binding proteins, OppF, was not required for peptide transport or for sporulation. The OppA peptide-binding protein, which is periplasmically located in Gram-negative species, has a signal sequence characteristic of lipoproteins with an amino-terminal lipo-amino acid anchor. Cellular location studies revealed that OppA was associated with the cell during exponential growth, but was released into the medium in stationary phase. A major role of the Opp system in Gram-negative bacteria is the recycling of cell-wall peptides as they are released from the growing peptidoglycan. We postulate that the accumulation of such peptides may play a signalling role in the initiation of sporulation, and that the sporulation defect in opp mutants results from an inability to transport these peptides.
authors.affiliation: Department of Molecular and Experimental Medicine, Research Institute of Scripps Clinic, La Jolla, California 92037.
authors.forename: M
authors.initials: M
authors.lastname: Perego
authors.forename: C F
authors.initials: CF
authors.lastname: Higgins
authors.forename: S R
authors.initials: SR
authors.lastname: Pearce
authors.forename: M P
authors.initials: MP
authors.lastname: Gallagher
authors.forename: J A
authors.initials: JA
authors.lastname: Hoch
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000235:genetics / Q000502:physiology*; D001426:Bacterial Proteins / Q000235:genetics; D001483:Base Sequence; D001692:Biological Transport; D015153:Blotting, Western; D002352:Carrier Proteins; D016386:Chromosome Walking; D008040:Genetic Linkage; D008074:Lipoproteins / Q000235:genetics; D026901:Membrane Transport Proteins / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D009842:Oligopeptides / Q000378:metabolism*; D009876:Operon; D010641:Phenotype; D015183:Restriction Mapping; D013171:Spores, Bacterial
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D008074:Lipoproteins; D026901:Membrane Transport Proteins; D009842:Oligopeptides; C046506:oligopeptide-binding protein, bacteria; C037230:oligopeptide permease, Bacteria