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

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

DOI

  • Nina Kronqvist, Karolinska Institutet, Sverige
  • Martins Otikovs, Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis, Aizkraukles 21, Riga , Letland
  • Volodymyr Chmyrov, Royal Institute of Technology, Sverige
  • Gefei Chen, Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai CN-201620, Kina
  • Marlene Andersson, Swedish University of Agricultural Sciences, Sverige
  • Kerstin Nordling, Karolinska Institutet, Sverige
  • Michael Landreh, Karolinska Institutet, Sverige
  • Médoune Sarr, Karolinska Institutet, Sverige
  • Hans Jörnvall, Karolinska Institutet, Sverige
  • Stefan Wennmalm, 1] Experimental Biomolecular Physics, Royal Institute of Technology-KTH, Albanova, SE-106 91 Stockholm, Sweden [2] Science for Life Laboratory, SE-171 65 Solna, Sverige
  • Jerker Widengren, Royal Institute of Technology, Sverige
  • Qing Meng, Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai CN-201620, Kina
  • Anna Rising, 1] KI Alzheimer Disease Research Centre, NVS Department, Karolinska Institutet, Novum, 5th floor, SE-141 86 Stockholm, Sweden [2] Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, The Biomedical Centre, SE-751 23 Uppsala, Sverige
  • Daniel Otzen
  • Stefan D Knight, Uppsala University, Sverige
  • Kristaps Jaudzems, Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis, Aizkraukles 21, Riga LV-1006, Letland
  • Jan Johansson, 1] KI Alzheimer Disease Research Centre, NVS Department, Karolinska Institutet, Novum, 5th floor, SE-141 86 Stockholm, Sweden [2] Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, The Biomedical Centre, SE-751 23 Uppsala, Sweden [3] Institute of Mathematics and Natural Sciences, Tallinn University, Narva mnt 25, EE-101 20 Tallinn, Estland
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.
OriginalsprogEngelsk
Artikelnummer3254
TidsskriftNature Communications
Vol/bind5
Antal sider11
ISSN2041-1723
DOI
StatusUdgivet - 10 feb. 2014

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