Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein

Dominika T. Gruszka, Fiona Whelan, Oliver E. Farrance, Herman K. H. Fung, Emanuele Paci, Cy M. Jeffries, Dmitri I. Svergun, Clair Baldock, Christoph G. Baumann, David J. Brockwell, Jennifer R. Potts () and Jane Clarke ()
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Dominika T. Gruszka: University of Cambridge
Fiona Whelan: University of York
Oliver E. Farrance: Astbury Centre for Structural Molecular Biology, University of Leeds
Herman K. H. Fung: University of York
Emanuele Paci: Astbury Centre for Structural Molecular Biology, University of Leeds
Cy M. Jeffries: European Molecular Biology Laboratory, Hamburg Unit
Dmitri I. Svergun: European Molecular Biology Laboratory, Hamburg Unit
Clair Baldock: Faculty of Life Sciences, Wellcome Trust Centre for Cell-Matrix Research, University of Manchester
Christoph G. Baumann: University of York
David J. Brockwell: Astbury Centre for Structural Molecular Biology, University of Leeds
Jennifer R. Potts: University of York
Jane Clarke: University of Cambridge

Nature Communications, 2015, vol. 6, issue 1, 1-9

Abstract: Abstract Bacteria exploit surface proteins to adhere to other bacteria, surfaces and host cells. Such proteins need to project away from the bacterial surface and resist significant mechanical forces. SasG is a protein that forms extended fibrils on the surface of Staphylococcus aureus and promotes host adherence and biofilm formation. Here we show that although monomeric and lacking covalent cross-links, SasG maintains a highly extended conformation in solution. This extension is mediated through obligate folding cooperativity of the intrinsically disordered E domains that couple non-adjacent G5 domains thermodynamically, forming interfaces that are more stable than the domains themselves. Thus, counterintuitively, the elongation of the protein appears to be dependent on the inherent instability of its domains. The remarkable mechanical strength of SasG arises from tandemly arrayed ‘clamp’ motifs within the folded domains. Our findings reveal an elegant minimal solution for the assembly of monomeric mechano-resistant tethers of variable length.

Date: 2015
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DOI: 10.1038/ncomms8271

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