Taurine suppresses liquid–liquid phase separation of lysozyme protein | Zendy

Kanae Tsubotani | Zendy; Sayuri Maeyama | Zendy; Shigeru Murakami | Zendy; Stephen W. Schaffer | Zendy; Takashi Ito | Zendy

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Taurine suppresses liquid–liquid phase separation of lysozyme protein

Author(s) -

Kanae Tsubotani,

Sayuri Maeyama,

Shigeru Murakami,

Stephen W. Schaffer,

Takashi Ito

Publication year - 2021

Publication title -

amino acids

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.894

H-Index - 118

eISSN - 1438-2199

pISSN - 0939-4451

DOI - 10.1007/s00726-021-02980-2

Subject(s) - lysozyme , osmolyte , taurine , chemistry , polyethylene glycol , ribonuclease , chromatography , ovalbumin , biochemistry , biology , amino acid , rna , immune system , immunology , gene

Taurine is a compatible osmolyte that confers stability to proteins. Recent studies have revealed that liquid-liquid phase separation (LLPS) of proteins underlie the formation of membraneless organelles in cells. In the present study, we evaluated the role of taurine on LLPS of hen egg lysozyme. We demonstrated that taurine decreases the turbidity of the polyethylene glycol-induced crowding solution of lysozyme. We also demonstrated that taurine attenuates LLPS-dependent cloudiness of lysozyme solution with 0.5 or 1 M NaCl at a critical temperature. Moreover, we observed that taurine inhibits LLPS formation of a heteroprotein mix solution of lysozyme and ovalbumin. These data indicate that taurine can modulate the formation of LLPS of proteins.

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