Characterization of Lysine Monomethylome and Methyltransferase in Model Cyanobacterium Synechocystis sp. PCC 6803.
10.1016/j.gpb.2019.04.005
- Author:
Xiaohuang LIN
1
,
2
,
3
;
Mingkun YANG
1
,
4
;
Xin LIU
1
,
2
,
3
;
Zhongyi CHENG
5
;
Feng GE
1
,
6
Author Information
1. State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China
2. Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China
3. University of Chinese Academy of Sciences, Beijing 100039, China.
4. Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China.
5. Jingjie PTM BioLab (Hangzhou) Co. Ltd, Hangzhou 310018, China.
6. Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China. Electronic address: gefeng@ihb.ac.cn.
- Publication Type:Research Support, Non-U.S. Gov't
- Keywords:
Aspartate aminotransferase;
Cyanobacteria;
Lysine methyltransferase;
Lysine monomethylation;
Post-translational modification
- MeSH:
Bacterial Proteins/metabolism*;
Lysine/metabolism*;
Methyltransferases/metabolism*;
Photosynthesis;
Protein Processing, Post-Translational;
Synechocystis/growth & development*
- From:
Genomics, Proteomics & Bioinformatics
2020;18(3):289-304
- CountryChina
- Language:English
-
Abstract:
Protein lysine methylation is a prevalent post-translational modification (PTM) and plays critical roles in all domains of life. However, its extent and function in photosynthetic organisms are still largely unknown. Cyanobacteria are a large group of prokaryotes that carry out oxygenic photosynthesis and are applied extensively in studies of photosynthetic mechanisms and environmental adaptation. Here we integrated propionylation of monomethylated proteins, enrichment of the modified peptides, and mass spectrometry (MS) analysis to identify monomethylated proteins in Synechocystis sp. PCC 6803 (Synechocystis). Overall, we identified 376 monomethylation sites in 270 proteins, with numerous monomethylated proteins participating in photosynthesis and carbon metabolism. We subsequently demonstrated that CpcM, a previously identified asparagine methyltransferase in Synechocystis, could catalyze lysine monomethylation of the potential aspartate aminotransferase Sll0480 both in vivo and in vitro and regulate the enzyme activity of Sll0480. The loss of CpcM led to decreases in the maximum quantum yield in primary photosystem II (PSII) and the efficiency of energy transfer during the photosynthetic reaction in Synechocystis. We report the first lysine monomethylome in a photosynthetic organism and present a critical database for functional analyses of monomethylation in cyanobacteria. The large number of monomethylated proteins and the identification of CpcM as the lysine methyltransferase in cyanobacteria suggest that reversible methylation may influence the metabolic process and photosynthesis in both cyanobacteria and plants.
