Global Profiling of 2-hydroxyisobutyrylome in Common Wheat
- Author:
Zhang NING
1
;
Zhang LINGRAN
;
Li LINJIE
;
Geng JUNYOU
;
Zhao LEI
;
Ren YAN
;
Dong ZHONGDONG
;
Chen FENG
Author Information
1. National Key Laboratory of Wheat and Maize Crop Science/Agronomy College,Henan Agricultural University,Zhengzhou 450046,China
- Keywords:
Post-translational modification;
Lysine 2-hydroxyisobutyrylation;
Common wheat;
Proteomics;
Co-immunoprecipitation
- From:
Genomics, Proteomics & Bioinformatics
2022;20(4):688-701
- CountryChina
- Language:Chinese
-
Abstract:
As a novel post-translational modification(PTM),lysine 2-hydroxyisobutyrylation(Khib)is considered to regulate gene transcriptional activities in eukaryotic cells;however,the functions of Khib-modified proteins in plants remain unknown.Here,we report that Khib is an evolutionarily-conserved PTM in wheat and its progenitors.A total of 3348 Khib sites on 1074 proteins are iden-tified in common wheat(Triticum aestivum L.)by using affinity purification and mass spectroscopy of 2-hydroxyisobutyrylome.Bioinformatic data indicate that Khib-modified proteins participate in a wide variety of biological and metabolic pathways.Immunoprecipitation confirms that Khib-modified proteins are present endogenously.A comparison of Khib and other main PTMs shows that Khib-modified proteins are simultaneously modified by multiple PTMs.Using mutagenesis experiments and co-immunoprecipitation assays,we demonstrate that Khib on K206 of phospho-glycerate kinase(PGK)is a key regulatory modification for its enzymatic activity,and mutation on K206 affects the interactions of PGK with its substrates.Furthermore,Khib modification of low-molecular-weight proteins is a response to the deacetylase inhibitors nicotinamide and tricho-statin.This study provides evidence to promote our current understanding of Khib in wheat plants,including the cooperation between Khib and its metabolic regulation.
