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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

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Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. / Kronqvist, Nina; Otikovs, Martins; Chmyrov, Volodymyr et al.

I: Nature Communications, Bind 5, 3254, 10.02.2014.

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

Harvard

Kronqvist, N, Otikovs, M, Chmyrov, V, Chen, G, Andersson, M, Nordling, K, Landreh, M, Sarr, M, Jörnvall, H, Wennmalm, S, Widengren, J, Meng, Q, Rising, A, Otzen, D, Knight, SD, Jaudzems, K & Johansson, J 2014, 'Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation', Nature Communications, bind 5, 3254. https://doi.org/10.1038/ncomms4254

APA

Kronqvist, N., Otikovs, M., Chmyrov, V., Chen, G., Andersson, M., Nordling, K., Landreh, M., Sarr, M., Jörnvall, H., Wennmalm, S., Widengren, J., Meng, Q., Rising, A., Otzen, D., Knight, S. D., Jaudzems, K., & Johansson, J. (2014). Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. Nature Communications, 5, [3254]. https://doi.org/10.1038/ncomms4254

CBE

Kronqvist N, Otikovs M, Chmyrov V, Chen G, Andersson M, Nordling K, Landreh M, Sarr M, Jörnvall H, Wennmalm S, et al. 2014. Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. Nature Communications. 5:Article 3254. https://doi.org/10.1038/ncomms4254

MLA

Kronqvist, Nina et al. "Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation". Nature Communications. 2014. 5. https://doi.org/10.1038/ncomms4254

Vancouver

Kronqvist N, Otikovs M, Chmyrov V, Chen G, Andersson M, Nordling K et al. Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. Nature Communications. 2014 feb. 10;5:3254. doi: 10.1038/ncomms4254

Author

Kronqvist, Nina ; Otikovs, Martins ; Chmyrov, Volodymyr et al. / Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. I: Nature Communications. 2014 ; Bind 5.

Bibtex

@article{4c1f585e6bf646c5a0863792ed306300,
title = "Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation",
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.",
author = "Nina Kronqvist and Martins Otikovs and Volodymyr Chmyrov and Gefei Chen and Marlene Andersson and Kerstin Nordling and Michael Landreh and M{\'e}doune Sarr and Hans J{\"o}rnvall and Stefan Wennmalm and Jerker Widengren and Qing Meng and Anna Rising and Daniel Otzen and Knight, {Stefan D} and Kristaps Jaudzems and Jan Johansson",
year = "2014",
month = feb,
day = "10",
doi = "10.1038/ncomms4254",
language = "English",
volume = "5",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation

AU - Kronqvist, Nina

AU - Otikovs, Martins

AU - Chmyrov, Volodymyr

AU - Chen, Gefei

AU - Andersson, Marlene

AU - Nordling, Kerstin

AU - Landreh, Michael

AU - Sarr, Médoune

AU - Jörnvall, Hans

AU - Wennmalm, Stefan

AU - Widengren, Jerker

AU - Meng, Qing

AU - Rising, Anna

AU - Otzen, Daniel

AU - Knight, Stefan D

AU - Jaudzems, Kristaps

AU - Johansson, Jan

PY - 2014/2/10

Y1 - 2014/2/10

N2 - 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.

AB - 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.

U2 - 10.1038/ncomms4254

DO - 10.1038/ncomms4254

M3 - Journal article

C2 - 24510122

VL - 5

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 3254

ER -