| Literature DB >> 11741876 |
Erh-Min Lai1, Ralf Eisenbrandt, Markus Kalkum, Erich Lanka, Clarence I Kado.
Abstract
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.Entities:
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Year: 2002 PMID: 11741876 PMCID: PMC134783 DOI: 10.1128/JB.184.1.327-330.2002
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490