Protein arginine methylation: Cellular functions and methods of analysis

Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Biochimica et Biophysica Acta (Impact Factor: 4.66). 01/2007; 1764(12):1890-903. DOI: 10.1016/j.bbapap.2006.08.008
Source: PubMed


During the last few years, new members of the growing family of protein arginine methyltransferases (PRMTs) have been identified and the role of arginine methylation in manifold cellular processes like signaling, RNA processing, transcription, and subcellular transport has been extensively investigated. In this review, we describe recent methods and findings that have yielded new insights into the cellular functions of arginine-methylated proteins, and we evaluate the currently used procedures for the detection and analysis of arginine methylation.

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    • "The functions of histone lysine methylation in plant biological processes are involved in floral organ development, flowering transition, shoot and root branching, endodormancy release, carotenoid biosynthesis, hormone regulation, thigmomorphogenesis, and fungal pathogens resistance (Dong et al., 2008; Cazzonelli et al., 2009, 2014; Berr et al., 2010a,b; Sui et al., 2012; Sun et al., 2012; Kim et al., 2013a; Saito et al., 2015). Moreover, histone methylation also occurs at arginine residues and histone arginine methylation is involved in many cellular processes including transcription, RNA processing and transport, signaling, subcellular transport and so on (Pahlich et al., 2006). Histone arginine methylation is controlled by a conserved protein family named protein arginine methyltransferases (PRMTs). "
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    ABSTRACT: In eukaryotes, histone acetylation and methylation have been known to be involved in regulating diverse developmental processes and plant defense. These histone modification events are controlled by a series of histone modification gene families. To date, there is no study regarding genome-wide characterization of histone modification related genes in citrus species. Based on the two recent sequenced sweet orange genome databases, a total of 136 CsHMs (Citrus sinensis histone modification genes), including 47 CsHMTs (histone methyltransferase genes), 23 CsHDMs (histone demethylase genes), 50 CsHATs (histone acetyltransferase genes), and 16 CsHDACs (histone deacetylase genes) were identified. These genes were categorized to 11 gene families. A comprehensive analysis of these 11 gene families was performed with chromosome locations, phylogenetic comparison, gene structures, and conserved domain compositions of proteins. In order to gain an insight into the potential roles of these genes in citrus fruit development, 42 CsHMs with high mRNA abundance in fruit tissues were selected to further analyze their expression profiles at six stages of fruit development. Interestingly, a numbers of genes were expressed highly in flesh of ripening fruit and some of them showed the increasing expression levels along with the fruit development. Furthermore, we analyzed the expression patterns of all 136 CsHMs response to the infection of blue mold (Penicillium digitatum), which is the most devastating pathogen in citrus post-harvest process. The results indicated that 20 of them showed the strong alterations of their expression levels during the fruit-pathogen infection. In conclusion, this study presents a comprehensive analysis of the histone modification gene families in sweet orange and further elucidates their behaviors during the fruit development and the blue mold infection responses.
    Frontiers in Plant Science 08/2015; 6:607. DOI:10.3389/fpls.2015.00607 · 3.95 Impact Factor
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    • "Thus, RNA-binding proteins are key regulators of parasite function. RNA-binding proteins constitute a large number of arginine methylated proteins in higher organisms (Pahlich et al. 2006; Bedford and Clarke 2009), and this prompted us to examine the arginine methylome of T. brucei to ask if the same is true in this early-branching eukaryote. Indeed, in a global proteomics screen in T. brucei , we identified 136 RNA-binding and metabolic proteins harboring arginine methylmarks (Fisk et al. 2013; Lott et al. 2013). "
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    ABSTRACT: Arginine methylation is a common posttranslational modification that has far-reaching cellular effects. Trypanosoma brucei is an early-branching eukaryote with four characterized protein arginine methyltransferases (PRMTs), one additional putative PRMT, and over 800 arginine methylated proteins, suggesting that arginine methylation has widespread impacts in this organism. While much is known about the activities of individual T. brucei PRMTs (TbPRMTs), little is known regarding how TbPRMTs function together in vivo. In this study, we analyzed single and selected double TbPRMT knockdowns for the impact on expression of TbPRMTs and global methylation status. Repression of TbPRMT1 caused a decrease in asymmetric dimethylarginine and a marked increase in monomethylarginine that was catalyzed by TbPRMT7, suggesting that TbPRMT1 and TbPRMT7 can compete for the same substrate. We also observed an unexpected and strong interdependence between TbPRMT1 and TbPRMT3 protein levels. This finding, together with the observation of similar methyl landscape profiles in TbPRMT1 and TbPRMT3 repressed cells, strongly suggests that these two enzymes form a functional complex. We show that corepression of TbPRMT6/7 synergistically impacts growth of procyclic-form T. brucei. Our findings also implicate the actions of noncanonical, and as yet unidentified, PRMTs in T. brucei. Together, our studies indicate that TbPRMTs display a functional interplay at multiple levels.
    MicrobiologyOpen 10/2014; 3(5). DOI:10.1002/mbo3.191 · 2.21 Impact Factor
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    • "The change of arginine side chain guanidino groups is quantitatively one of the most extensive protein methylation reactions in mammalian cells [14]. Arginine is unique among amino acids as its guanidino group contains five potential hydrogen bond donors that are positioned for favorable interactions with biological hydrogen bond acceptors [15] [16]. "
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    ABSTRACT: α-Defensins (e.g. human neutrophil peptides, HNPs) have a broad spectrum bactericidal activity contributing to human innate immunity. The positive charge of amino acid side chains is responsible for the first interaction of cationic antimicrobial peptides with negatively charged bacterial membranes. α-Defensins contain a high content of Arg residues compared to Lys. In this paper, different peptide analogs including substitution of Arg-14 respectively with N(G)-N(G')-asymmetric dimethyl-l-arginine (ADMA), N(G)-N(G')-symmetric dimethyl-l-arginine (SDMA) and Lys (R14K and R15KR14KR15K) variants have been studied to test the role of Arg guanidino group and the localized cationic charge of Lys for interaction with lipid membranes. Our findings show that all the variants have a decreased disruptive activity against the bilayer. The methylated analogs show a reduction in membrane partitioning due to the lack of their ability to form hydrogen bonds. Comparison with the native HNP-1 peptide has been discussed.
    Biophysical chemistry 04/2014; 190-191C:32-40. DOI:10.1016/j.bpc.2014.04.003 · 1.99 Impact Factor
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