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Arabidopsis protein methylome

Monomethylation, Dimethylation, Trimethylation in Arabidopsis thaliana

621 modifications in 513 peptides, found in 933 proteins

Experiment Details

Exp 123


Experimental Setup
Tissue10-day old seedlings
ConditionControl conditions
PTM EnrichmentPTMScan® Methyl arginine immunoaffinity beads (Cell Signaling Technology) and Anti-methyllysine ant
MS InstrumentOrbitrap Fusion
MS/MS Search Parameters
Protein DatabaseArabidopsis_tha database (31,392 accessions)
Decoy StrategyReverse
FDR Threshold0.01
Search Algorithm(s)MaxQuant (version 1.5.2.8)
Precursor Mass Tolerance20 ppm
PTM Site AllocationPTM Score
Identification ScoreMaxQuant Score
ProteaseTrypsin
Fixed ModificationsCarbamidomethyl (C)
Variable ModificationsMethylation (KR)
Dimethylation (KR)
Trimethylation (KR)
Oxidation (M)
Other Information
CommentsLysine and Argingine monomethylation. Table S1 to S6. Asymmetric and symmetric Arginine dimethylation are unified here under the PTM type 'Dimethylation' (Me2).


Publication Information

Liang et al., 2020

PubMed ID: 31809900

No external accession available

Abstract

J Proteomics. 2020 Feb 20;213:103601. doi: 10.1016/j.jprot.2019.103601. Epub 
2019 Dec 3.

Protein methylome analysis in Arabidopsis reveals regulation in RNA-related 
processes.

Liang Q(1), Geng Q(1), Jiang L(1), Liang M(2), Li L(2), Zhang C(3), Wang W(4).

Author information:
(1)Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, 
Beijing 100081, China.
(2)Jingjie PTM BioLab (Hangzhou) Co.Ltd, Hangzhou 310018, China.
(3)Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, 
Beijing 100081, China. Electronic address: zhangchunyi@caas.cn.
(4)Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, 
Beijing 100081, China. Electronic address: wangweixuan@caas.cn.

Protein methylation has been proposed as an important post-translational 
modification, which occurs predominantly on lysine and arginine residues. Recent 
discoveries have revealed that protein methylation is also present on 
non-histones besides histones, and plays critical roles in regulating protein 
stability and function. However, proteome-wide identification of methylated 
proteins in plants remains unexplored. Here, we present the first global survey 
of monomethyl arginine, symmetric and asymmetric dimethyl arginine, and 
monomethyl, dimethyl, trimethyl lysine modifications in the proteomes of 
10-day-old Arabidopsis seedlings through a combination of immunoaffinity 
purification and mass spectrometry analysis. In total, we identified 617 
methylation sites which mapped to 412 proteins, with 263 proteins harboring 381 
lysine methylation sites and 149 proteins harboring 236 arginine methylation 
sites. Among them, 607 methylation sites on 408 proteins were novel findings. 
Motif analysis revealed that glycine preferentially flanked methylated arginine 
residues, whereas aspartate and glutamate enriched around mono- and dimethylated 
lysine sites. Methylated proteins were involved in a variety of metabolic 
processes, showing significant enrichment in RNA-related metabolic pathways 
including spliceosome, RNA transport, and ribosome. Our data provide a global 
view of methylated non-histone proteins in Arabidopsis, laying foundations for 
elucidating the biological function of protein methylation in plants. 
SIGNIFICANCE: Protein methylation has emerged as a common and important 
modification both in eukaryotes and prokaryotes. The identification of 
methylated sites/peptides is fundamental for further functional analysis of 
protein methylation. This study was the first proteome-scale identification of 
lysine and arginine methylation in plants. We found that methylation occurred 
widely on non-histone proteins in Arabidopsis and was involved in diverse 
biological functions. The results provide foundations for the investigation of 
the protein methylome in Arabidopsis and provide powerful resources for the 
functional analysis of protein methylation in plants.

Copyright © 2019 Elsevier B.V. All rights reserved.

DOI: 10.1016/j.jprot.2019.103601
PMID: 31809900 [Indexed for MEDLINE]