2022 Fiscal Year Annual Research Report
Elucidation of effect of phase separation on conformation and dynamics of spider silk proteins
| Project/Area Number |
20K15738
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| Research Institution | Institute of Physical and Chemical Research |
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Principal Investigator |
Oktaviani NA 国立研究開発法人理化学研究所, 環境資源科学研究センター, 基礎科学特別研究員 (70753838)
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| Project Period (FY) |
2020-04-01 – 2023-03-31
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| Keywords | NMR / spider silk protein / LLPS / mechanism |
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| Outline of Annual Research Achievements |
In the final fiscal year, the effect of phase separation on conformation and dynamics of the repetitive domain and full length minispidroin NR6C and NR12C were investigated. The tyrosine residue of the repetitive domain was affected upon LLPS phenomenon. Then, we made a mutant on the repetitive domain which substituted the tyrosine with serine residue. We found a drastic effect on the mutant, where the oligomerization was suppressed at higher kPi concentration, suggesting the important role of tyrosine residues in promoting oligomerization upon LLPS phenomenon. Overall, upon phase separation at higher kPi concentration, spider silk protein forms oligomers. The repetitive domain is getting more rigid at higher kPi concentration. The C-terminal domain (CTD) and tyrosine from the repetitive domain are important as stickers which mediate the oligomerization on the LLPS formation. Both domains work synergistically to promote oligomerization upon liquid-liquid phase separation. This phenomenon mediates the self-assembly of soluble spider dragline silk protein into insoluble hierarchical fiber.
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Research Products
(5 results)
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[Journal Article] 1000 spider silkomes: Linking sequences to silk physical properties2022
Author(s)
K Arakawa, N Kono, AD Malay, A Tateishi, N Ifuku, H Masunaga, R Sato, K Tsuchiya,..., NA Oktaviani, RC Preda, NM Pugno, R Rajhkowa, X Wang, K Yazawa, Z Zheng, K Numata
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Journal Title
Science advances
Volume: 8
Pages: 6043
DOI
Peer Reviewed
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