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J Biol Chem, Vol. 274, Issue 32, 22548-22555, August 6, 1999
From the Max-Planck-Institut für Molekulare Genetik,
Ihnestrasse 73, Dahlem, D-14195 Berlin, Germany and
§ Davis Crown Gall Group, University of California,
Davis, California 95616
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.
Conjugative Pili of IncP Plasmids, and the Ti Plasmid T Pilus
Are Composed of Cyclic Subunits
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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