Premium
Nonenzymatic acetylation of ubiquitin Lys side chains is modulated by their neighboring residues
Author(s) -
Lee SeoYeon,
Choi YunSeok,
Kim EunHee,
Cheong HaeKap,
Lee YunJu,
Lee JinGu,
Ye Yihong,
Ryu KyoungSeok
Publication year - 2018
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14404
Subject(s) - acetylation , ubiquitin , chemistry , side chain , mutagenesis , molecule , biochemistry , stereochemistry , organic chemistry , mutation , polymer , gene
Nonenzymatic acetylation of Lys side chains (Lys‐ SC s) by various in vivo reactive molecules has been suggested to play novel regulatory roles. Ubiquitin ( UB ) has seven Lys residues that are utilized for synthesis of specific poly‐ UB chains. To understand the nature of these Lys‐ SC modifications, the chemical acetylation rate and p K a and Hill coefficient of each UB ‐Lys‐ SC were measured. Mutagenesis studies combined with the determination of activation energy indicated that specific neighboring residues of the Lys‐ SC s have a potential catalytic activity during nonenzymatic acetylation. Based on the shared chemistry between nonenzymatic Lys acetylation and ubiquitylation, the characterized chemical properties of the UB ‐Lys‐ SC s could be a reference for deciphering both mechanisms. Our NMR approaches could be useful for studying general nonenzymatic Lys acylations of various proteins.