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Self-assembly of spider silk proteins is controlled by a pH-sensitive relay

Author

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  • Glareh Askarieh

    (Oslo University, 1033 Blindern, 0315 Oslo, Norway
    Uppsala BioCenter, SLU, Biomedical Centre, P.O. Box 590, SE-751 24 Uppsala, Sweden)

  • My Hedhammar

    (Physiology and Biochemistry, SLU, Biomedical Centre, P.O. Box 575, SE-751 23 Uppsala, Sweden)

  • Kerstin Nordling

    (Physiology and Biochemistry, SLU, Biomedical Centre, P.O. Box 575, SE-751 23 Uppsala, Sweden)

  • Alejandra Saenz

    (Complutense University of Madrid)

  • Cristina Casals

    (Complutense University of Madrid)

  • Anna Rising

    (Physiology and Biochemistry, SLU, Biomedical Centre, P.O. Box 575, SE-751 23 Uppsala, Sweden)

  • Jan Johansson

    (Physiology and Biochemistry, SLU, Biomedical Centre, P.O. Box 575, SE-751 23 Uppsala, Sweden)

  • Stefan D. Knight

    (Uppsala BioCenter, SLU, Biomedical Centre, P.O. Box 590, SE-751 24 Uppsala, Sweden)

Abstract

Spider silk's dual identity Many proteins form fibrillar structures at high concentrations, but spider silk proteins, with highly repetitive segments flanked by non-repetitive (NR) terminal domains, behave differently. They are remarkably soluble when stored at high concentration yet can convert to extremely sturdy fibres on demand. The molecular mechanism that makes this possible is not yet clear, but two structural studies in this issue provide new clues. Askarieh et al. present the 1.7 Å X-ray crystal structure of the N-terminal domain of a dragline spidroin from the nursery web spider Euprosthenops australis. The structure shows how this highly conserved domain can regulate silk assembly by preventing premature aggregation of spidroins and triggering polymerization as the pH falls along the silk extrusion duct. Hagn et al. determined the solution structure of the C-terminal NR domain of the dragline silk protein fibroin 3 from the common orb-weaver Araneus diadematus. They observe a conformational switch, activated by chemical or mechanical stimuli, between storage and assembly forms of the protein.

Suggested Citation

  • Glareh Askarieh & My Hedhammar & Kerstin Nordling & Alejandra Saenz & Cristina Casals & Anna Rising & Jan Johansson & Stefan D. Knight, 2010. "Self-assembly of spider silk proteins is controlled by a pH-sensitive relay," Nature, Nature, vol. 465(7295), pages 236-238, May.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7295:d:10.1038_nature08962
    DOI: 10.1038/nature08962
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    Cited by:

    1. Jingyao Li & Bojing Jiang & Xinyuan Chang & Han Yu & Yichao Han & Fuzhong Zhang, 2023. "Bi-terminal fusion of intrinsically-disordered mussel foot protein fragments boosts mechanical strength for protein fibers," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Jianming Chen & Arata Tsuchida & Ali D. Malay & Kousuke Tsuchiya & Hiroyasu Masunaga & Yui Tsuji & Mako Kuzumoto & Kenji Urayama & Hirofumi Shintaku & Keiji Numata, 2024. "Replicating shear-mediated self-assembly of spider silk through microfluidics," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    3. Tina Arndt & Kristaps Jaudzems & Olga Shilkova & Juanita Francis & Mathias Johansson & Peter R. Laity & Cagla Sahin & Urmimala Chatterjee & Nina Kronqvist & Edgar Barajas-Ledesma & Rakesh Kumar & Gefe, 2022. "Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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