@article{132226,
  keywords = {Models, Molecular, Bacterial Proteins, Mutation, Molecular Sequence Data, Binding Sites, Membrane Proteins, Mass Spectrometry, Cell Membrane, Peptide Hydrolases, Bacillus subtilis, Protein Stability, Fimbriae Proteins, Fimbriae, Bacterial, Transformation, Bacterial},
  author = {Jessica Mann and Valerie Carabetta and Ileana Cristea and David Dubnau},
  title = {Complex formation and processing of the minor transformation pilins of Bacillus subtilis},
  abstract = {<p>Transformation in most bacteria is dependent on orthologues of Type 2 secretion and Type 4 pilus system proteins. In each system, pilin proteins (major and minor) are required to make the pilus structure and are essential to the process, although the precise roles of the minor pilins remain unclear. We have explored protein-protein interactions among the competence minor pilins of Bacillus subtilis through in vitro binding studies, immunopurification and mass spectrometry. We demonstrate that the minor pilins directly interact, and the minor pilin ComGG interacts with most of the known proteins required for transformation. We find that ComGG requires other ComG proteins for its stabilization and for processing by the pre-pilin peptidase. These observations, C-terminal mutations in ComGG that prevent processing and the inaccessibility of pre-ComGG to externally added protease suggest a model in which pre-ComGG must be associated with other minor pilins for processing to take place. We propose that ComGG does not become a transmembrane protein until after processing. These behaviours contrast with that of pre-ComGC, the major pilin, which is accessible to externally added protease and requires only the peptidase to be processed. The roles of the pilins and of the pilus in transformation are discussed.</p>
},
  year = {2013},
  journal = {Mol Microbiol},
  volume = {90},
  pages = {1201-15},
  month = {12/2013},
  issn = {1365-2958},
  doi = {10.1111/mmi.12425},
  language = {eng},
}