Evolutionary conservation and post-translational control of S-adenosyl-L-homocysteine hydrolase in land plants
Physcomitrella patens
Protein methylation
Hydrolase
DOI:
10.1371/journal.pone.0227466
Publication Date:
2020-07-17T17:25:39Z
AUTHORS (8)
ABSTRACT
Trans-methylation reactions are intrinsic to cellular metabolism in all living organisms. In land plants, a range of substrate-specific methyltransferases catalyze the methylation DNA, RNA, proteins, cell wall components and numerous species-specific metabolites, thereby providing means for growth acclimation various terrestrial habitats. consume vast amounts S-adenosyl-L-methionine (SAM) as methyl donor several compartments. The inhibitory reaction by-product, S-adenosyl-L-homocysteine (SAH), is continuously removed by SAH hydrolase (SAHH), which essentially maintains trans-methylation cells. Here we report on evolutionary conservation post-translational control SAHH plants. We provide evidence suggesting that forms oligomeric protein complexes phylogenetically divergent plants predominant complex composed tetramer enzyme. Analysis light-stress-induced adjustments Arabidopsis thaliana Physcomitrella patens further suggests regulatory actions may take place levels formation phosphorylation this metabolically central Collectively, these data suggest plant adaptation environments involved evolution mechanisms adjust machinery response environmental cues.
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