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Lysine methylation in cyanobacteria

ABSTRACT: Deciphering structure, function and mechanism of a new lysine methyltransferase cKMT1 in model cyanobacterium Synechocystis sp. PCC 6803

ORGANISM(S): Synechocystis Sp. Pcc 6803

SUBMITTER: Feng Ge

PROVIDER: PXD035617 | iProX | Fri Jul 29 00:00:00 BST 2022

REPOSITORIES: iProX

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

Cao Gaoxiang G Lin Xiaohuang X Ling Mingtian M Lin Jian J Zhang Qi Q Jia Kun K Chen Bainan B Wei Wei W Wang Min M Jia Shuzhao S Yang Mingkun M Ge Feng F

Molecular & cellular proteomics : MCP 20230228 4

Lysine methylation is a conserved and dynamic regulatory posttranslational modification performed by lysine methyltransferases (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 t ...[more]

PMID: 36858286

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