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Biogenesis of T Pili in Agrobacterium tumefaciens Requires Precise VirB2 Propilin Cleavage and Cyclization

Erh-Min Lai,^1, Ralf Eisenbrandt,^2, Markus Kalkum,^2, Erich Lanka,² and Clarence I. Kado^1*

Davis Crown Gall Group, University of California, Davis, California 95616,¹ Max-Planck-Institut für Molekulare Genetik, D-14195 Berlin, Germany²

Received 16 August 2001/ Accepted 10 October 2001

VirB2 propilin is processed by the removal of a 47-amino-acid signal peptide to generate a 74-amino-acid peptide product in both Escherichia coli and Agrobacterium tumefaciens. The cleaved VirB2 protein is further cyclized to form the T pilin in A. tumefaciens but not in E. coli. Mutations in the signal peptidase cleavage sequence of VirB2 propilin cause the formation of aberrant T pilin and also severely attenuate virulence. No T pilus was observed in these mutants. The potential role of the exact VirB2 propilin cleavage and cyclization in T pilus biogenesis and virulence is discussed.

Present address: Department of Biology, University of Michigan, Ann Arbor, MI 48109-1048.

Present address: Biochemie GmbH, A-6250 Kundl, Austria.

Present address: Department for Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10021-6399.

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