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Journal of Bacteriology, January 2002, p. 327-330, Vol. 184, No. 1
0021-9193/01/$04.00+0 DOI: 10.1128/JB.184.1.327-330.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Ralf Eisenbrandt,2,
Markus Kalkum,2,
Erich Lanka,2 and Clarence I. Kado1*
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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