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First comprehensive proteomics analysis of lysine crotonylation in leaves of peanut ( Arachis hypogaea L.)
Author(s) -
Xu Manlin,
Luo Jianda,
Li Ying,
Shen Lili,
Zhang Xia,
Yu Jing,
Guo Zhiqing,
Wu Juxiang,
Chi Yucheng,
Yang Jinguang
Publication year - 2021
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.202000156
Subject(s) - lysine , chloroplast , biochemistry , proteomics , biology , ribosome , photosynthesis , arachis hypogaea , amino acid , botany , gene , rna
Lysine crotonylation is an important post‐translational modification process. Most research in this area has been carried out on mammals and yeast, but there has been little research on it in plants. In the current study, large‐scale lysine crotonylome analysis was performed by a combination of affinity enrichment and high‐resolution LC‐MS/MS analysis. Altogether, 6051 lysine crotonylation sites were identified in 2508 protein groups. Bioinformatics analysis showed that lysine‐crotonylated proteins were involved in many biological processes, such as carbon fixation in photosynthetic organisms, biosynthesis of amino acids, ribosomes structure and function. In particular, subcellular localization analysis showed that 43% of the crotonylated proteins were located in the chloroplast. Twenty‐nine crotonylation proteins were associated with photosynthesis and functional enrichment that these proteins were associated with the reaction center, photosynthetic electron transport, and ATP synthesis. Based on these results, further studies to expand on the lysine crotonylome analysis were suggested.