cKMT1 is a New Lysine Methyltransferase That Methylates the Ferredoxin-NADP(+) Oxidoreductase and Regulates Energy Transfer in Cyanobacteria

doi:10.1016/j.mcpro.2023.100521

YIC-IR

	cKMT1 is a New Lysine Methyltransferase That Methylates the Ferredoxin-NADP(+) Oxidoreductase and Regulates Energy Transfer in Cyanobacteria
	Cao, Gaoxiang 1,2,3; Lin, Xiaohuang 1,2; Ling, Mingtian 1,2; Lin, Jian 1,2; Zhang, Qi 1,2; Jia, Kun 1,2; Chen, Bainan 1,2; Wei, Wei 1,2; Wang, Min 4; Jia, Shuzhao 4; Yang, Mingkun 1,2; Ge, Feng 1,2
发表期刊	MOLECULAR & CELLULAR PROTEOMICS
	2023-04-01
卷号	22 期号:4 页码:20
DOI	10.1016/j.mcpro.2023.100521
通讯作者	Yang, Mingkun([email protected]) ; Ge, Feng([email protected])
英文摘要	Lysine methylation is a conserved and dynamic regulatory posttranslational modification performed by lysine meth-yltransferases (KMTs). KMTs catalyze the transfer of mono-, di-, or tri-methyl groups to substrate proteins and play a critical regulatory role in all domains of life. To date, only one KMT has been identified in cyanobacteria. Here, we tested all of the predicted KMTs in the cyanobacterium Synechocystis sp. PCC 6803 (Synechocystis), and we biochemically characterized sll1526 that we termed cKMT1 (cyanobacterial lysine methyltransferase 1) and determined that it can catalyze lysine methylation both in vivo and in vitro. Loss of cKMT1 alters photosynthetic electron transfer in Synechocystis. We analyzed cKMT1-regulated methylation sites in Synechocystis using a tim-sTOF Pro instrument. We identified 305 class I lysine methylation sites within 232 proteins, and of these, 80 methylation sites in 58 proteins were hypomethylated in Delta cKMT1 cells. We further demonstrated that cKMT1 could methylate ferredoxin-NADP(+) oxidoreductase (FNR) and its potential sites of action on FNR were identified. Amino acid residues H118 and Y219 were identified as key resi-dues in the putative active site of cKMT1 as indicated by structure simulation, site-directed mutagenesis, and KMT activity measurement. Using mutations that mimic the unmethylated forms of FNR, we demonstrated that the inability to methylate K139 residues results in a decrease in the redox activity of FNR and affects energy transfer in Synechocystis. Together, our study identified a new KMT in Synechocystis and elucidated a methylation-mediated molecular mechanism catalyzed by cKMT1 for the regu-lation of energy transfer in cyanobacteria.
资助机构	China Postdoctoral Science Foundation ; State Key Laboratory of Fresh-water Ecology and Biotechnology
收录类别	SCI
语种	英语
关键词[WOS]	SYNECHOCOCCUS SP PCC-7002 ; CYCLIC ELECTRON FLOW ; PHOTOSYSTEM-I ; STRUCTURAL INSIGHTS ; ANALYSIS REVEALS ; POSTTRANSLATIONAL MODIFICATIONS ; THYLAKOID MEMBRANES ; PROTEIN METHYLATION ; EXCITATION-ENERGY ; STATE TRANSITIONS
研究领域[WOS]	Biochemistry & Molecular Biology
WOS记录号	WOS:001002371300001
引用统计	被引频次：2[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.yic.ac.cn/handle/133337/34824
专题	中国科学院烟台海岸带研究所
通讯作者	Yang, Mingkun; Ge, Feng
作者单位	1.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan, Peoples R China 2.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan, Peoples R China 3.Univ Chinese Acad Sci, Beijing, Peoples R China 4.Chinese Acad Sci, Inst Hydrobiol, Anal & Testing Ctr, Wuhan, Peoples R China
推荐引用方式 GB/T 7714	Cao, Gaoxiang,Lin, Xiaohuang,Ling, Mingtian,et al. cKMT1 is a New Lysine Methyltransferase That Methylates the Ferredoxin-NADP(+) Oxidoreductase and Regulates Energy Transfer in Cyanobacteria[J]. MOLECULAR & CELLULAR PROTEOMICS,2023,22(4):20.
APA	Cao, Gaoxiang.,Lin, Xiaohuang.,Ling, Mingtian.,Lin, Jian.,Zhang, Qi.,...&Ge, Feng.(2023).cKMT1 is a New Lysine Methyltransferase That Methylates the Ferredoxin-NADP(+) Oxidoreductase and Regulates Energy Transfer in Cyanobacteria.MOLECULAR & CELLULAR PROTEOMICS,22(4),20.
MLA	Cao, Gaoxiang,et al."cKMT1 is a New Lysine Methyltransferase That Methylates the Ferredoxin-NADP(+) Oxidoreductase and Regulates Energy Transfer in Cyanobacteria".MOLECULAR & CELLULAR PROTEOMICS 22.4(2023):20.