The N-terminal domains of spider silk proteins assemble ultrafast and protected from charge screening

Simone Schwarze, Fabian U. Zwettler, Christopher M. Johnson and Hannes Neuweiler ()
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Simone Schwarze: Julius-Maximilians-University Würzburg, Am Hubland, 97074 Würzburg, Germany
Fabian U. Zwettler: Julius-Maximilians-University Würzburg, Am Hubland, 97074 Würzburg, Germany
Christopher M. Johnson: Medical Research Council Laboratory of Molecular Biology
Hannes Neuweiler: Julius-Maximilians-University Würzburg, Am Hubland, 97074 Würzburg, Germany

Nature Communications, 2013, vol. 4, issue 1, 1-7

Abstract: Abstract Web spiders assemble spidroin monomers into silk fibres of unrivalled tensile strength at remarkably high spinning speeds of up to 1 m s−1. The spidroin N-terminal domain contains a charge-driven, pH-sensitive relay that controls self-association by an elusive mechanism. The underlying kinetics have not yet been reported. Here we engineer a fluorescence switch into the isolated N-terminal domain from spidroin 1 of the major ampullate gland of the nursery web spider E. australis that monitors dimerization. We observe ultrafast association that is surprisingly insensitive to salt, contrasting the classical screening effects in accelerated, charged protein interfaces. To gain deeper mechanistic insight, we mutate each of the protonatable residue side chains and probe their contributions. Two vicinal aspartic acids are critically involved in an unusual process of accelerated protein association that is protected from screening by electrolytes, potentially facilitating the rapid synthesis of silk fibres by web spiders.

Date: 2013
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DOI: 10.1038/ncomms3815

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