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Halophilic to mesophilic adaptation of ubiquitin‐like proteins
Author(s) -
Li Quan,
Li Mengqing,
Li Cong,
Li Xinxin,
Lu Chenghui,
Tu Xiaoming,
Zhang Zhiyong,
Zhang Xuecheng
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14023
Subject(s) - mesophile , halophile , mutagenesis , adaptation (eye) , amino acid substitution , biochemistry , ubiquitin , protein folding , biology , chemistry , substitution (logic) , flexibility (engineering) , mutation , genetics , bacteria , gene , statistics , mathematics , neuroscience , computer science , programming language
Elucidating how proteins adapt from halophilic to mesophilic environments will enable a better understanding of protein evolution and folding. In this study, by directed evolution and site‐directed mutagenesis of the halophilic ubiquitin‐like protein (ULP) Samp2, we find that substitution of the prebiotic amino acid Asp31 by Gly is uniquely effective in the mesophilic adaptation of ULP. Sequence analysis shows that substitution of Asp/Glu in halophilic ULPs by Gly in mesophilic ULPs has higher occurrence than other substitutions, supporting the unique role of the substitution in the mesophilic adaptation of ULP. Molecular dynamic simulations indicate that the mesophilic adaptation might result from the effect of the substitution on the conformational flexibility of ULP.