Human protein arginine methyltransferases in vivo – distinct properties of eight canonical members of the PRMT family

Herrmann, Frank; Pably, Peter; Eckerich, Carmen; Bedford, Mark T.; Fackelmayer, Frank O.

doi:10.1242/jcs.039933

Cited by 129 publications

(131 citation statements)

References 65 publications

(119 reference statements)

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“…Mutagenesis-Mouse PRMT7-pEGFP-C1 plasmid was prepared as described (6). The wild-type plasmid was mutated to create a catalytically inactive enzyme that cannot bind AdoMet, with motif I residues LDIG changed to AAAA.…”

Section: Methodsmentioning

confidence: 99%

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Mammalian Protein Arginine Methyltransferase 7 (PRMT7) Specifically Targets RXR Sites in Lysine- and Arginine-rich Regions

Feng¹,

Maity

Whitelegge³

et al. 2013

Journal of Biological Chemistry

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159

212

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Background: Protein arginine methyltransferase 7 (PRMT7) is associated with various functions and diseases, but its substrate specificity is poorly defined. Results: Insect cell-expressed PRMT7 forms -monomethylarginine residues at basic RXR sequences in peptides and histone H2B. Conclusion: PRMT7 is a type III PRMT with a unique substrate specificity. Significance: Novel post-translational modification sites generated by PRMT7 may regulate biological function.

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Section: Methodsmentioning

confidence: 99%

“…In humans and mice, PRMT7 is a 692-amino acid protein with an ancestral duplication of the catalytic domains, both of which are required for its activity (4). PRMT7, when expressed as a GFP fusion protein, shows a predominantly cytoplasmic distribution (6).…”

mentioning

confidence: 99%

Mammalian Protein Arginine Methyltransferase 7 (PRMT7) Specifically Targets RXR Sites in Lysine- and Arginine-rich Regions

Feng¹,

Maity

Whitelegge³

et al. 2013

Journal of Biological Chemistry

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159

212

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“…Arginine methylation is accomplished by a family of protein arginine methyltransferases (PRMTs) that can transfer a methyl group from S-adenosylmethionine to the guanido nitrogens of arginine residues (1). PRMTs are classified into three distinct types (type I-III) on the basis of the location and the type of monomethylarginine or dimethylarginine they introduce.…”

Section: Introductionmentioning

confidence: 99%

The role of protein arginine-methyltransferase 1 in gliomagenesis

Wang

Tan²,

Yang³

et al. 2012

BMB Reports

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Protein arginine methyltransferase 1 (PRMT1), a type-I arginine methyltransferase, has been implicated in diverse cellular events. We have focused on the role of PRMT1 in gliomagenesis. In this study, we showed that PRMT1 expression was up-regulated in glioma tissues and cell lines compared with normal brain tissues. The knock-down of PRMT1 resulted in an arrest in the G1-S phase of the cell cycle, proliferation inhibition and apoptosis induction in four glioma cell lines (T98G, U87MG, U251, and A172). Moreover, an in vivo study confirmed that the tumor growth in nude mouse xenografts was significantly decreased in the RNAi-PRMT1 group. Additionally, we found that the level of the asymmetric dimethylated modification of H4R3, a substrate of PRMT1, was higher in glioma cells than in normal brain tissues and decreased after PRMT1 knock-down. Our data suggest a potential role for PRMT1 as a novel biomarker of and therapeutic target in gliomas. [BMB Reports 2012; 45(8): [470][471][472][473][474][475]

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“…epigenetics | protein-protein complex | A9145C P osttranslational methylation of lysine and arginine residues by protein lysine methyltransferases and protein arginine methyltransferases (PRMTs) alters the activity and interactions of substrate proteins, with crucial consequences to diverse cellular functions (1)(2)(3). Histone methylation is an epigenetic mark that plays a vital role in normal cell function, and whose dysregulation is associated with several diseases (4).…”

mentioning

confidence: 99%

Crystal structure of the human PRMT5:MEP50 complex

Antonysamy

Bonday

Campbell

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

285

385

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Protein arginine methyltransferases (PRMTs) play important roles in several cellular processes, including signaling, gene regulation, and transport of proteins and nucleic acids, to impact growth, differentiation, proliferation, and development. PRMT5 symmetrically di-methylates the two-terminal ω-guanidino nitrogens of arginine residues on substrate proteins. PRMT5 acts as part of a multimeric complex in concert with a variety of partner proteins that regulate its function and specificity. A core component of these complexes is the WD40 protein MEP50/WDR77/p44, which mediates interactions with binding partners and substrates. We have determined the crystal structure of human PRMT5 in complex with MEP50 (methylosome protein 50), bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4. The structure of the surprising hetero-octameric complex reveals the close interaction between the seven-bladed β-propeller MEP50 and the N-terminal domain of PRMT5, and delineates the structural elements of substrate recognition.epigenetics | protein-protein complex | A9145C P osttranslational methylation of lysine and arginine residues by protein lysine methyltransferases and protein arginine methyltransferases (PRMTs) alters the activity and interactions of substrate proteins, with crucial consequences to diverse cellular functions (1-3). Histone methylation is an epigenetic mark that plays a vital role in normal cell function, and whose dysregulation is associated with several diseases (4).The PRMT family of methyltransferases belongs to the largest class (class I) of S-adenosylmethionine (AdoMet)-dependent methyltransferase enzymes, responsible for the transfer of a methyl group from AdoMet to the arginine side-chains of histones and other proteins. PRMTs are further subdivided into type I, type II, type III, and type IV enzymes based on their patterns of arginine methylation. Eleven human PRMTs have been identified to date (5), and they all methylate the terminal guanidino nitrogen atoms of arginine residues. Type I PRMT enzymes (PRMT1, -2, -3, -4, -6, and -8) generate ω-NG-monomethyl and ω-NG,NG-asymmetric di-methyl arginines, whereas PRMT5 is a type II PRMT that catalyzes the formation of ω-NG-monomethyl and ω-NG,N′G-symmetric di-methyl arginine residues. PRMT7 was initially thought to have type II activity, but recent evidence suggests that it may be a type III enzyme that is only able to monomethylate substrates to form ω-NG-monomethyl arginine (6). A type IV enzyme that catalyses the formation of δ-N-methyl arginine has been identified in yeast (7). All PRMTs share the highly conserved methyltransferase catalytic domain, and several PRMTs contain additional domains that modulate their activity and specificity. PRMT2, PRMT3, and PRMT9 contain SH3, zinc finger, and TRP2 domains, respectively, and PRMT5 contains a largely uncharacterized N-terminal region.In contrast to type I PRMTs, PRMT5 functions as part of various high molecular weight protein complexes that invariably contain the WD-repe...

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Human protein arginine methyltransferases in vivo – distinct properties of eight canonical members of the PRMT family

Cited by 129 publications

References 65 publications

Mammalian Protein Arginine Methyltransferase 7 (PRMT7) Specifically Targets RXR Sites in Lysine- and Arginine-rich Regions

Mammalian Protein Arginine Methyltransferase 7 (PRMT7) Specifically Targets RXR Sites in Lysine- and Arginine-rich Regions

The role of protein arginine-methyltransferase 1 in gliomagenesis

Crystal structure of the human PRMT5:MEP50 complex

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