Arginine Methylation of Scaffold Attachment Factor A by Heterogeneous Nuclear Ribonucleoprotein Particle-associated PRMT1

Herrmann, Frank; Bossert, Maike; Schwander, Andrea; Akgün, Ercan; Fackelmayer, Frank O.

doi:10.1074/jbc.m407332200

Cited by 63 publications

(57 citation statements)

References 44 publications

(40 reference statements)

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“…HMGA1a Associates with and Is in Vivo Methylated by PRMT6-Certain PRMTs have been shown to interact with their substrates (39,40). To demonstrate that HMGA1a can associate in vitro with PRMT6, a blot overlay was employed using wild-type HMGA1a along with several deletion mutants.…”

Section: Resultsmentioning

confidence: 99%

The AT-hook of the Chromatin Architectural Transcription Factor High Mobility Group A1a Is Arginine-methylated by Protein Arginine Methyltransferase 6

Sgarra

Lee

Tessari

et al. 2006

Journal of Biological Chemistry

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The HMGA1a protein belongs to the high mobility group A (HMGA) family of architectural nuclear factors, a group of proteins that plays an important role in chromatin dynamics. HMGA proteins are multifunctional factors that associate both with DNA and nuclear proteins that have been involved in several nuclear processes, such as transcriptional regulation, viral integration, DNA repair, RNA processing, and chromatin remodeling. The activity of HMGA proteins is finely modulated by a variety of post-translational modifications. Arginine methylation was recently demonstrated to occur on HMGA1a protein, and it correlates with the apoptotic process and neoplastic progression. Methyltransferases responsible for these modifications are unknown. Here we show that the protein arginine methyltransferase PRMT6 specifically methylates HMGA1a protein both in vitro and in vivo. By mass spectrometry, the sites of methylation were unambiguously mapped to Arg 57 and Arg 59 , two residues which are embedded in the second AT-hook, a region critical for both protein-DNA and protein-protein interactions and whose modification may cause profound alterations in the HMGA network. The in vivo association of HMGA and PRMT6 place this yet functionally uncharacterized methyltransferase in the well established functional context of the chromatin structure organization.

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Section: Resultsmentioning

confidence: 99%

The AT-hook of the Chromatin Architectural Transcription Factor High Mobility Group A1a Is Arginine-methylated by Protein Arginine Methyltransferase 6

Sgarra

Lee

Tessari

et al. 2006

Journal of Biological Chemistry

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“…PRMT1 is the most prevalent and conserved member of type I PRMT methyltransferases, which transfer either one or two methyl groups from an appropriate donor to a single guanidino nitrogen on a protein-internal arginine residue leading either to a monomethylarginine (MMA) or an asymmetric dimethylarginine (aDMA) (Bedford and Clarke 2009;Yu 2011). Although PRMT1 was already indicated to catalyze the modification of several hnRNPs (Nichols et al 2000;Wada et al 2002;Herrmann et al 2004;Passos et al 2006), we here present a complementary set of data demonstrating that PRMT1 is necessary and sufficient to catalyze the observed methylation pattern of AUF1 p45 (Fig. 3).…”

Section: Discussionmentioning

confidence: 99%

Arginine methylation enhances the RNA chaperone activity of the West Nile virus host factor AUF1 p45

Friedrich

Schmidt

Schierhorn

et al. 2016

RNA

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A prerequisite for the intracellular replication process of the Flavivirus West Nile virus (WNV) is the cyclization of the viral RNA genome, which enables the viral replicase to initiate RNA synthesis. Our earlier studies indicated that the p45 isoform of the cellular AU-rich element binding protein 1 (AUF1) has an RNA chaperone activity, which supports RNA cyclization and viral RNA synthesis by destabilizing a stem structure at the WNV RNA's 3 ′ -end. Here we show that in mammalian cells, AUF1 p45 is consistently modified by arginine methylation of its C terminus. By a combination of different experimental approaches, we can demonstrate that the methyltransferase PRMT1 is necessary and sufficient for AUF1 p45 methylation and that PRMT1 is required for efficient WNV replication. Interestingly, in comparison to the nonmethylated AUF1 p45, the methylated AUF1 p45 aDMA exhibits a significantly increased affinity to the WNV RNA termini. Further data also revealed that the RNA chaperone activity of AUF1 p45 aDMA is improved and the methylated protein stimulates viral RNA synthesis considerably more efficiently than the nonmethylated AUF1 p45. In addition to its destabilizing RNA chaperone activity, we identified an RNA annealing activity of AUF1 p45, which is not affected by methylation. Arginine methylation of AUF1 p45 thus represents a specific determinant of its RNA chaperone activity while functioning as a WNV host factor. Our data suggest that the methylation modifies the conformation of AUF1 p45 and in this way affects its RNA binding and restructuring activities.

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“…With regard to the regulation of gene expression, arginine methylation appears to act as an epigenetic mark on chromatin, similar to lysine methylation, which contributes to the histone code and affects expression of the underlying genomic information. In this case, methylated arginines on histones (reviewed by Ruthenburg et al, 2007), and possibly non-histone proteins involved in nuclear architecture (Fackelmayer, 2005a;Herrmann et al, 2004), are recognized by protein adaptors termed 'effectors', which contain domains that specifically bind to methylated arginine (or lysine) residues. Well-characterized examples for these domains or 'modules' are the chromodomain, tudor domain or the PHD finger (reviewed by Ruthenburg et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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

Herrmann

Pably

Eckerich

et al. 2009

Journal of Cell Science

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114

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Methylation of arginine residues is a widespread post-translational modification of proteins catalyzed by a small family of protein arginine methyltransferases (PRMTs). Functionally, the modification appears to regulate protein functions and interactions that affect gene regulation, signalling and subcellular localization of proteins and nucleic acids. All members have been, to different degrees, characterized individually and their implication in cellular processes has been inferred from characterizing substrates and interactions. Here, we report the first comprehensive comparison of all eight canonical members of the human PRMT family with respect to subcellular localization and dynamics in living cells. We show that the individual family members differ significantly in their properties, as well as in their substrate specificities, suggesting that they fulfil distinctive, non-redundant functions in vivo. In addition, certain PRMTs display different subcellular localization in different cell types, implicating cell- and tissue-specific mechanisms for regulating PRMT functions.

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Arginine Methylation of Scaffold Attachment Factor A by Heterogeneous Nuclear Ribonucleoprotein Particle-associated PRMT1

Cited by 63 publications

References 44 publications

The AT-hook of the Chromatin Architectural Transcription Factor High Mobility Group A1a Is Arginine-methylated by Protein Arginine Methyltransferase 6

The AT-hook of the Chromatin Architectural Transcription Factor High Mobility Group A1a Is Arginine-methylated by Protein Arginine Methyltransferase 6

Arginine methylation enhances the RNA chaperone activity of the West Nile virus host factor AUF1 p45

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

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