Group3LEAペプチドのタンパク質凝集抑制メカニズムに関する実験的研究

山川 賢太郎; 古木 隆生; 古田 忠臣; 畑中 理恵; 黄川田 隆洋; 丹羽 達也; 田口 英樹; 古澤 宏幸; 岡畑 恵雄; 櫻井 実

doi:10.20585/cryobolcryotechnol.59.2_95

Experimental Study on the Mechanism Underlying the Anti-aggregation Function of a Group3LEA Peptide

Kentaro YAMAKAWA, Takao FURUKI, Tadaomi FURUTA, Rie HATANAKA, Takahiro KIKAWADA, Tatsuya NIWA, Hideki TAGUCHI, Hiroyuki FURUSAWA, Yoshio OKAHATA, Minoru SAKURAI

Author information

Kentaro YAMAKAWA
Center for Biological Resources and Informatics, Tokyo Institute of Technology
Takao FURUKI
Center for Biological Resources and Informatics, Tokyo Institute of Technology
Tadaomi FURUTA
Center for Biological Resources and Informatics, Tokyo Institute of Technology
Rie HATANAKA
National Institute of Agrobiological Sciences(NIAS)
Takahiro KIKAWADA
National Institute of Agrobiological Sciences(NIAS)
Tatsuya NIWA
Department of Biomolecular Engineering, Tokyo Institute of Technology
Hideki TAGUCHI
Department of Biomolecular Engineering, Tokyo Institute of Technology
Hiroyuki FURUSAWA
Department of Biomolecular Engineering, Tokyo Institute of Technology
Yoshio OKAHATA
Department of Biomolecular Engineering, Tokyo Institute of Technology
Minoru SAKURAI
Center for Biological Resources and Informatics, Tokyo Institute of Technology

Keywords: LEA protein, desiccation tolerance, aggregation

JOURNAL FREE ACCESS

2013 Volume 59 Issue 2 Pages 95-99

DOI https://doi.org/10.20585/cryobolcryotechnol.59.2_95

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Abstract

We show that a short model peptide which has two tandem repeats of the 11-mer motif of a group3 late embryogenesis abundant protein protects proteins against aggregation by desiccation stress. Next, we measure the dissociation constant between the LEA model peptide and its partner protein (lysozyme and HybD) using quartz crystal microbalance (QCM) method. Similar experiments are performed for a native LEA protein from the anhydrobiotic nematode A. avenae. On the basis of these results, the mechanism of the anti-aggregation function of the LEA peptide is discussed.

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