Evolutionary conservation and post-translational control of S-adenosyl-L-homocysteine hydrolase in land plants

PloS One
Sara AlegreSaijaliisa Kangasjärvi

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 of DNA, RNA, proteins, cell wall components and numerous species-specific metabolites, thereby providing means for growth and acclimation in various terrestrial habitats. Trans-methylation reactions consume vast amounts of S-adenosyl-L-methionine (SAM) as a methyl donor in several cellular compartments. The inhibitory reaction by-product, S-adenosyl-L-homocysteine (SAH), is continuously removed by SAH hydrolase (SAHH), which essentially maintains trans-methylation reactions in all living cells. Here we report on the evolutionary conservation and post-translational control of SAHH in land plants. We provide evidence suggesting that SAHH forms oligomeric protein complexes in phylogenetically divergent land plants and that the predominant protein complex is composed by a tetramer of the enzyme. Analysis of light-stress-induced adjustments of SAHH in Arabidopsis thaliana and Physcomitrella patens further suggests that regulatory actions may take place on the levels of protein complex formation and phosphorylation of this metabolically central enzyme. Coll...Continue Reading

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Methods Mentioned

BETA
gel filtration
transgenic
acetylation
electrophoresis
chip
confocal microscopy
Confocal
ubiquitination

Software Mentioned

BioEdit
PhosphoRS filter
R Studio
Decoy Database Search
GENEVESTIGATOR
Zeiss Zen
ClustalW Multiple Alignment
R package pheatmap
Fiji
Mascot

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