Work

Conjugative Pili of IncP Plasmids, and the Ti Plasmid T Pilus Are Composed of Cyclic Subunits

Year: 1999

Type: article

Abstract: TrbC propilin is the precursor of the pilin subunit TrbC of IncP conjugative pili in Escherichia coli. Likewise, its homologue, VirB2 propilin, is processed into T pilin of the Ti plasmid T pilus in Agrobacterium tumefaciens. TrbC and VirB2 propilin are truncated post-translationally at the N terminus by the removal of a 36/47-residue leader peptide, respectively. TrbC propilin undergoes a second processing step by the removal of 27 residues at the C terminus by host-encoded functions followed by the excision of four additional C-terminal residues by a plasmid-borne serine protease. The final product TrbC of 78 residues is cyclized via an intramolecular covalent head-to-tail peptide bond. The T pilin does not undergo additional truncation but is likewise cyclized. The circular structures of these pilins, as verified by mass spectrometry, represent novel primary configurations that conform and assemble into the conjugative apparatus.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.274.32.22548

Authors: Ralf Eisenbrandt, Markus Kalkum, Erh-Min Lai, Rudi Lurz, Clarence I. Kado, Erich Lanka

Institutions: Max Planck Institute for Molecular Genetics, University of California, Davis

Language: English

Topic: Bacterial Genetics and Biotechnology

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: Deutsche Forschungsgemeinschaft, Bundesministerium für Bildung und Forschung, University of California, Davis, National Institute of General Medical Sciences