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  • 1. Di Yu, Xiao
    et al.
    Dubnovitsky, Anatoly
    Institutionen för molekylärbiologi - (slu).
    Pudney, Alex F.
    MacIntyre, Sheila
    Knight, Stefan D.
    Institutionen för molekylärbiologi - (slu) .
    Zavialov, Anton V.
    Institutionen för molekylärbiologi - (slu) .
    Allosteric Mechanism Controls Traffic in the Chaperone/Usher Pathway2012In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 20, no 11, p. 1861-1871Article in journal (Refereed)
    Abstract [en]

    Many virulence organelles of Gram-negative bacterial pathogens are assembled via the chaperone/usher pathway. The chaperone transports organelle subunits across the periplasm to the outer membrane usher, where they are released and incorporated into growing fibers. Here, we elucidate the mechanism of the usher-targeting step in assembly of the Yersinia pestis F1 capsule at the atomic level. The usher interacts almost exclusively with the chaperone in the chaperone:subunit complex. In free chaperone, a pair of conserved proline residues at the beginning of the subunit-binding loop form a "proline lock" that occludes the usher-binding surface and blocks usher binding. Binding of the subunit to the chaperone rotates the proline lock away from the usher-binding surface, allowing the chaperone-subunit complex to bind to the usher. We show that the proline lock exists in other chaperone/usher systems and represents a general allosteric mechanism for selective targeting of chaperone:subunit complexes to the usher and for release and recycling of the free chaperone.

  • 2.
    Di Yu, Xiao
    et al.
    Swedish Univ Agr Sci, Dept Mol Biol, Uppsala Bioctr, BMC, SE-75324 Uppsala, Sweden..
    Fooks, Laura J.
    Univ Reading, Sch Biol Sci, Reading RG6 6AJ, Berks, England..
    Moslehi-Mohebi, Elham
    Univ Reading, Sch Biol Sci, Reading RG6 6AJ, Berks, England..
    Tischenko, Vladimir M.
    Inst Biol Instrumentat, Pushchino 142292, Russia..
    Askarieh, Gelareh
    Swedish Univ Agr Sci, Dept Mol Biol, Uppsala Bioctr, BMC, SE-75324 Uppsala, Sweden..
    Knight, Stefan D.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology. Swedish Univ Agr Sci, Dept Mol Biol, Uppsala Bioctr, BMC, SE-75324 Uppsala, Sweden..
    MacIntyre, Sheila
    Univ Reading, Sch Biol Sci, Reading RG6 6AJ, Berks, England..
    Zavialov, Anton V.
    Swedish Univ Agr Sci, Dept Mol Biol, Uppsala Bioctr, BMC, SE-75324 Uppsala, Sweden.;Univ Turku, Dept Chem, FIN-20520 Turku, Finland..
    Large Is Fast, Small Is Tight: Determinants of Speed and Affinity in Subunit Capture by a Periplasmic Chaperone2012In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 417, no 4, p. 294-308Article in journal (Refereed)
    Abstract [en]

    The chaperone/usher pathway assembles surface virulence organelles of Gram-negative bacteria, consisting of fibers of linearly polymerized protein subunits. Fiber subunits are connected through 'donor strand complementation': each subunit completes the immunoglobulin (Ig)-like fold of the neighboring subunit by donating the seventh beta-strand in trans. Whereas the folding of Ig domains is a fast first-order process, folding of Ig modules into the fiber conformation is a slow second-order process. Periplasmic chaperones separate this process in two parts by forming transient complexes with subunits. Interactions between chaperones and subunits are also based on the principle of donor strand complementation. In this study, we have performed mutagenesis of the binding motifs of the Caf1M chaperone and Caf1 capsular subunit from Yersinia pestis and analyzed the effect of the mutations on the structure, stability, and kinetics of Caf1M-Caf1 and Caf1-Caf1 interactions. The results suggest that a large hydrophobic effect combined with extensive main-chain hydrogen bonding enables Caf1M to rapidly bind an early folding intermediate of Caf1 and direct its partial folding. The switch from the Caf1M-Caf1 contact to the less hydrophobic, but considerably tighter and less dynamic Caf1-Caf1 contact occurs via the zip-out-zip-in donor strand exchange pathway with pocket 5 acting as the initiation site. Based on these findings, Caf1M was engineered to bind Caf1 faster, tighter, or both faster and tighter. To our knowledge, this is the first successful attempt to rationally design an assembly chaperone with improved chaperone function.

  • 3.
    Roy, Saumendra P.
    et al.
    Department of Molecular Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences, Uppsala, Sweden.
    Rahman, Mohammad M.
    Di Yu, Xiao
    Department of Molecular Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences, Uppsala, Sweden.
    Tuittila, Minna
    Knight, Stefan D.
    Department of Molecular Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences, Uppsala, Sweden.
    Zavialov, Anton V.
    Department of Molecular Biology, Uppsala BioCenter, Swedish University of Agricultural Sciences, Uppsala, Sweden.
    Crystal structure of enterotoxigenic Escherichia coli colonization factor CS6 reveals a novel type of functional assembly2012In: Molecular Microbiology, ISSN 0950-382X, E-ISSN 1365-2958, Vol. 86, no 5, p. 1100-1115Article in journal (Refereed)
    Abstract [en]

    Coli surface antigen 6 (CS6) is a widely expressed enterotoxigenic Escherichia coli (ETEC) colonization factor that mediates bacterial attachment to the small intestinal epithelium. CS6 is a polymer of two protein subunits CssA and CssB, which are secreted and assembled on the cell surface via the CssC/CssD chaperone usher (CU) pathway. Here, we present an atomic resolution model for the structure of CS6 based on the results of X-ray crystallographic, spectroscopic and biochemical studies, and suggest a mechanism for CS6-mediated adhesion. We show that the CssA and CssB subunits are assembled alternately in linear fibres by the principle of donor strand complementation. This type of fibre assembly is novel for CU assembled adhesins. We also show that both subunits in the fibre bind to receptors on epithelial cells, and that CssB, but not CssA, specifically recognizes the extracellular matrix protein fibronectin. Taken together, structural and functional results suggest that CS6 is an adhesive organelle of a novel type, a hetero-polyadhesin that is capable of polyvalent attachment to different receptors.

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