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

Nina Kronqvist (), Martins Otikovs, Volodymyr Chmyrov, Gefei Chen, Marlene Andersson, Kerstin Nordling, Michael Landreh, Médoune Sarr, Hans Jörnvall, Stefan Wennmalm, Jerker Widengren, Qing Meng, Anna Rising, Daniel Otzen, Stefan D. Knight, Kristaps Jaudzems and Jan Johansson
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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
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
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

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms4254

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