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

التفاصيل البيبلوغرافية
العنوان: Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation
المؤلفون: Kronqvist, Nina, Otikovs, Martins, Chmyrov, Volodymyr, Chen, Gefei, Andersson, Marlene, Nordling, Kerstin, Landreh, Michael, Sarr, Médoune, Jörnvall, Hans, Wennmalm, Stefan, Widengren, Jerker, Meng, Qing, Rising, Anna, Otzen, Daniel Erik Rik, Knight, Stefan, Jaudzems, Kristaps, Johansson, Jan Ove
المصدر: Nature Communications. 5(1):3254
مصطلحات موضوعية: animal, biosynthesis, chemistry, dimerization, genetics, metabolism, nuclear magnetic resonance spectroscopy, pH, spectrofluorometry, spider, static electricity, Biological Physics, Biologisk fysik
الوصف: 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.
وصف الملف: electronic
URL الوصول: https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-187706
https://doi.org/10.1038/ncomms4254
https://kth.diva-portal.org/smash/get/diva2:931211/FULLTEXT01.pdf
قاعدة البيانات: SwePub
الوصف
تدمد:20411723
DOI:10.1038/ncomms4254