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

: Alegre S, Pascual J, Trotta A, Angeleri M, Rahikainen M, Brosche M, Moffatt B, Kangasjärvi S

Publisher: PUBLIC LIBRARY SCIENCE

: 2020

: PLoS ONE

: PLOS ONE

: ARTN e0227466

: 15

: 7

: 18

: 1932-6203

DOI: https://doi.org/10.1371/journal.pone.0227466(external)

: https://doi.org/10.1371/journal.pone.0227466(external)

: https://research.utu.fi/converis/portal/detail/Publication/49499378(external)

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 inArabidopsis thalianaandPhyscomitrella patensfurther suggests that regulatory actions may take place on the levels of protein complex formation and phosphorylation of this metabolically central enzyme. Collectively, these data suggest that plant adaptation to terrestrial environments involved evolution of regulatory mechanisms that adjust the trans-methylation machinery in response to environmental cues.

journal.pone.0227466.pdf