| Literature DB >> 33881613 |
Kanae Tsubotani1, Sayuri Maeyama1, Shigeru Murakami1, Stephen W Schaffer2, Takashi Ito3.
Abstract
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.Entities:
Keywords: Liquid–liquid phase separation; Lysozyme; Protein stability; Taurine
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Year: 2021 PMID: 33881613 DOI: 10.1007/s00726-021-02980-2
Source DB: PubMed Journal: Amino Acids ISSN: 0939-4451 Impact factor: 3.520