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Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation

Author

Listed:
  • Nina Kronqvist

    (KI Alzheimer Disease Research Centre, Karolinska Institutet)

  • Martins Otikovs

    (Latvian Institute of Organic Synthesis)

  • Volodymyr Chmyrov

    (Experimental Biomolecular Physics, Royal Institute of Technology—KTH, Albanova)

  • Gefei Chen

    (Institute of Biological Sciences and Biotechnology, Donghua University)

  • Marlene Andersson

    (Physiology and Biochemistry, Swedish University of Agricultural Sciences, The Biomedical Centre)

  • Kerstin Nordling

    (KI Alzheimer Disease Research Centre, Karolinska Institutet)

  • Michael Landreh

    (Karolinska Institutet)

  • Médoune Sarr

    (KI Alzheimer Disease Research Centre, Karolinska Institutet)

  • Hans Jörnvall

    (Karolinska Institutet)

  • Stefan Wennmalm

    (Experimental Biomolecular Physics, Royal Institute of Technology—KTH, Albanova
    Science for Life Laboratory)

  • Jerker Widengren

    (Experimental Biomolecular Physics, Royal Institute of Technology—KTH, Albanova)

  • Qing Meng

    (Institute of Biological Sciences and Biotechnology, Donghua University)

  • Anna Rising

    (KI Alzheimer Disease Research Centre, Karolinska Institutet
    Physiology and Biochemistry, Swedish University of Agricultural Sciences, The Biomedical Centre)

  • Daniel Otzen

    (Center for Insoluble Protein Structures (inSPIN), Aarhus University)

  • Stefan D. Knight

    (Uppsala University)

  • Kristaps Jaudzems

    (Latvian Institute of Organic Synthesis)

  • Jan Johansson

    (KI Alzheimer Disease Research Centre, Karolinska Institutet
    Physiology and Biochemistry, Swedish University of Agricultural Sciences, The Biomedical Centre
    Institute of Mathematics and Natural Sciences, Tallinn University)

Abstract

The mechanisms controlling the conversion of spider silk proteins into insoluble fibres, which happens in a fraction of a second and in a defined region of the silk glands, are still unresolved. The N-terminal domain changes conformation and forms a homodimer when pH is lowered from 7 to 6; however, the molecular details still remain to be determined. Here we investigate site-directed mutants of the N-terminal domain from Euprosthenops australis major ampullate spidroin 1 and find that the charged residues D40, R60 and K65 mediate intersubunit electrostatic interactions. Protonation of E79 and E119 is required for structural conversions of the subunits into a dimer conformation, and subsequent protonation of E84 around pH 5.7 leads to the formation of a fully stable dimer. These residues are highly conserved, indicating that the now proposed three-step mechanism prevents premature aggregation of spidroins and enables fast formation of spider silk fibres in general.

Suggested Citation

  • Nina Kronqvist & Martins Otikovs & Volodymyr Chmyrov & Gefei Chen & Marlene Andersson & Kerstin Nordling & Michael Landreh & Médoune Sarr & Hans Jörnvall & Stefan Wennmalm & Jerker Widengren & Qing Me, 2014. "Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation," Nature Communications, Nature, vol. 5(1), pages 1-11, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4254
    DOI: 10.1038/ncomms4254
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    Cited by:

    1. 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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