Halophilic to mesophilic adaptation of ubiquitin‐like proteins. Issue 4 (19th December 2020)

• Record Type: Journal Article
• Authors: Li, Quan; Li, Mengqing; Li, Cong; Li, Xinxin; Lu, Chenghui; Tu, Xiaoming; Zhang, Zhiyong; Zhang, Xuecheng
• Is Part Of: FEBS letters. Volume 595:Issue 4(2021)
• Page Start: 521
• Page End: 531
• Publication Date: 2020-12-19
• Subjects: conformational flexibility -- evolution -- mesophilic adaptation -- Samp2 -- ubiquitin‐like protein; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.14023
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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. Abstract :