Back to Search
Start Over
Biogenesis of T Pili in Agrobacterium tumefaciens Requires Precise VirB2 Propilin Cleavage and Cyclization
- Source :
- Journal of Bacteriology. 184:327-330
- Publication Year :
- 2002
- Publisher :
- American Society for Microbiology, 2002.
-
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.
- Subjects :
- Signal peptide
Virulence Factors
Virulence
Genetics and Molecular Biology
Protein Sorting Signals
Cleavage (embryo)
medicine.disease_cause
Microbiology
Pilus
Bacterial Proteins
medicine
Protein Precursors
Molecular Biology
Escherichia coli
Datura stramonium
Signal peptidase
biology
Serine Endopeptidases
Membrane Proteins
Agrobacterium tumefaciens
biochemical phenomena, metabolism, and nutrition
biology.organism_classification
Recombinant Proteins
Biochemistry
Fimbriae, Bacterial
Pilin
Mutation
biology.protein
bacteria
Fimbriae Proteins
Protein Processing, Post-Translational
Bacterial Outer Membrane Proteins
Subjects
Details
- ISSN :
- 10985530 and 00219193
- Volume :
- 184
- Database :
- OpenAIRE
- Journal :
- Journal of Bacteriology
- Accession number :
- edsair.doi.dedup.....e8bf687e8de80ad5637bb6b03de9aa2d