Root morphogenic pathways in Eucalyptus grandis are modified by the activity of protein arginine methyltransferases

Abstract

BackgroundMethylation of proteins at arginine residues, catalysed by members of the protein arginine methyltransferase (PRMT) family, is crucial for the regulation of gene transcription and for protein function in eukaryotic organisms. Inhibition of the activity of PRMTs in annual model plants has demonstrated wide-ranging involvement of PRMTs in key plant developmental processes, however, PRMTs have not been characterised or studied in long-lived tree species.ResultsTaking advantage of the recently available genome for Eucalyptus grandis, we demonstrate that most of the major plant PRMTs are conserved in E. grandis as compared to annual plants and that they are expressed in all major plant tissues. Proteomic and transcriptomic analysis in roots suggest that the PRMTs of E. grandis control a number of regulatory proteins and genes related to signalling during cellular/root growth and morphogenesis. We demonstrate here, using chemical inhibition of methylation and transgenic approaches, that plant type I PRMTs are necessary for normal root growth and branching in E. grandis. We further show that EgPRMT1 has a key role in root hair initiation and elongation and is involved in the methylation of β-tubulin, a key protein in cytoskeleton formation.ConclusionsTogether, our data demonstrate that PRMTs encoded by E. grandis methylate a number of key proteins and alter the transcription of a variety of genes involved in developmental processes. Appropriate levels of expression of type I PRMTs are necessary for the proper growth and development of E. grandis roots. Electronic supplementary materialThe online version of this article (doi:10.1186/s12870-017-1010-x) contains supplementary material, which is available to authorized users.

A Survey on Tubulin and Arginine Methyltransferase Families Sheds Light on P. lividus Embryo as Model System for Antiproliferative Drug Development

“…Recently, methylation has been found on tubulins occurring in lysine and arginine amino acid residues [22,75,76,77,78,79,80] and it has not been characterized in detail.…”

“…Recently, several lines of evidence [22,76,77,78] suggested that α- and β-tubulins undergo monomethylation or asymmetrical dimethylation in ω-N manner at specific arginine residues. To define methylation pattern occurring in P. lividus tubulins, sequence and pattern recognition analyses were carried out to map and characterize the amino acid residues putatively methylable and the kind of modification (monomethylarginine, MMA; asymmetric dimethylarginine, ADMA, or symmetric dimethylarginine, SDMA) (Table 5).…”

“…Methylation on R339 of some α-tubulin isotypes and R46, R62, R86, R162, R282, R318, R320 and R380 of some β-tubulin isotypes were recently shown by proteomics study of protein methylation (for details see Table 4) [22,76,77,78]. To provide a comprehensive survey of computed methylable aminoacid residues also in the light of physical constraints, we superpose the P. lividus tubulin 3D structures with human orthologues.…”

Protein arginine methyltransferases in protozoan parasites

“…PRMTs have also been identified in non-mammalian animals, filamentous fungi, yeasts, plants and protozoan parasites (McBride et al ., 2007; Ahmad et al ., 2011; Fisk and Read, 2011; Zhao et al ., 2016; Hadjikyriacou and Clarke, 2017; Plett et al ., 2017; Wang et al ., 2017; Bauer et al ., 2019). Enzymes similar to mammalian PRMT1, 3 and 5 are present in different eukaryotic organisms, whereas other PRMTs, such as PRMT2 and 8, are less conserved and it has been suggested that they could have evolved in the multicellular organisms as a requirement for tissue-specific functions (Bachand, 2007).…”

Protein arginine methylation: an emerging regulator of the cell cycle

“…CID5380390 and CID2818500 were found to produce the strongest inhibition with IC 50 values of 23 and 11 μM, respectively [ 209 ]. CID5380390 was used to characterize PRMT activity in E. grandis roots [ 211 ]. However, no further studies have been published on the mechanism of action for either of these inhibitors.…”