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The oligopeptide transport-system of bacillus-subtilis plays a role in the initiation of sporulation

Academic Article
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Overview

authors

  • Perego, Marta
  • Higgins, C. F.
  • Pearce, S. R.
  • Gallagher, M. P.
  • Hoch, James

publication date

  • January 1991

journal

  • Molecular Microbiology  Journal

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.

subject areas

  • Amino Acid Sequence
  • Bacillus subtilis
  • Bacterial Proteins
  • Base Sequence
  • Biological Transport
  • Blotting, Western
  • Carrier Proteins
  • Chromosome Walking
  • Genetic Linkage
  • Lipoproteins
  • Membrane Transport Proteins
  • Molecular Sequence Data
  • Mutation
  • Oligopeptides
  • Operon
  • Phenotype
  • Restriction Mapping
  • Spores, Bacterial
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Identity

International Standard Serial Number (ISSN)

  • 0950-382X

Digital Object Identifier (DOI)

  • 10.1111/j.1365-2958.1991.tb01838.x

PubMed ID

  • 1901616
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Additional Document Info

start page

  • 173

end page

  • 185

volume

  • 5

issue

  • 1

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