Donor strand complementation mechanism in the biogenesis of non-pilus systems

The F1 antigen of Yersinia pestis belongs to a class of non-pilus adhesins assembled via a classical chaperone-usher pathway. Such pathways consist of PapD-like chaperones that bind subunits and pilot them to the outer membrane usher, where they are assembled into surface structures. In a recombinant Escherichia coli model system, chaperone-subunit (Caf1M:Caf1n) complexes accumulate in the periplasm. Three independent methods showed that these complexes are rod- or coil-shaped linear arrays of Caf1 subunits capped at one end by a single copy of Caf1M chaperone. Deletion and point mutagenesis identified an N-terminal donor strand region of Caf1 that was essential for polymerization in vitro, in the periplasm and at the cell surface, but not for chaperone-subunit interaction. Partial protease digestion of periplasmic complexes revealed that this region becomes buried upon formation of Caf1:Caf1 contacts. These results show that, despite the capsule-like appearance of F1 antigen, the basic structure is assembled as a linear array of subunits held together by intersubunit donor strand complementation. This example shows that strikingly different architectures can be achieved by the same general principle of donor strand complementation and suggests that a similar basic polymer organization will be shared by all surface structures assembled by classical chaperone-usher pathways.

Zavialov A.V.1 , Kersley J.2 , Korpela T.3 , Zav'yalov V.P. 4 , MacIntyre S.2 , Knight S.D.1
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  • 1 Department of Molecular Biology, Uppsala Biomedical Center, Swedish University of Agricultural Sciences, SE-753 24 Uppsala, Sweden
  • 2 Microbiology Division, School of Animal and Microbial Sciences, University of Reading, Reading RG6 6AJ, United Kingdom
  • 3 Finnish-Russian Joint Biotechnology Laboratory, University of Turku, BioCity, FIN-20520 Turku, Finland
  • 4 Department of Biomedical Technologies, Medical Faculty, Russian University of the Friendship of Peoples, 117198 Moscow, Russian Federation
Ключевые слова
adhesin; antigen; chaperone; outer membrane protein; protein subunit; proteinase; recombinant protein; amino terminal sequence; article; biogenesis; cell surface; complex formation; cytoplasm; DNA microarray; Escherichia coli; gene deletion; genetic complementation; in vitro study; nonhuman; outer membrane; point mutation; polymerization; priority journal; protein binding; protein protein interaction; surface property; Yersinia pestis; Amino Acid Sequence; Bacterial Proteins; Base Sequence; Biopolymers; DNA Primers; Fimbriae, Bacterial; Genetic Complementation Test; Molecular Chaperones; Molecular Sequence Data; Periplasm; Sequence Homology, Amino Acid; Escherichia coli; Negibacteria; Yersinia; Yersinia pestis
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Dao L.D., Rabinovich S.A., Van Ha N.
Бюллетень экспериментальной биологии и медицины Клеточные технологии в биологии и медицине. New York Consultants BureauSpringer / Автономная некоммерческая организация Издательство Российской академии медицинских наук. Том 134. 2002. С. 379-381