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In Vivo and In Vitro Arginine Methylation of RNA-Binding Proteins

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Liu, Qing, Dreyfuss, Gideon·1995·Molecular and Cellular Biology

Abstract

Heterogenous nuclear ribonucleoproteins (hnRNPs) bind pre-mRNAs and facilitate their processing into mRNAs. Many of the hnRNPs undergo extensive posttranslational modifications including methylation on arginine residues. hnRNPs contain about 65% of the total NG,NG-dimethylarginine found in the cell nucleus. The role of this modification is not known. Here we identify the hnRNPs that are methylated in HeLa cells and demonstrate that most of the pre-mRNA-binding proteins receive this modification. Using recombinant human hnRNP A1 as a substrate, we have partially purified and characterized a protein-arginine N-methyltransferase specific for hnRNPs from HeLa cells. This methyltransferase can methylate the same subset of hnRNPs in vitro as are methylated in vivo. Furthermore, it can also methylate other RNA-binding proteins that contain the RGG motif RNA-binding domain. This activity is evolutionarily conserved from lower eukaryotes to mammals, suggesting that methylation has a significant role in the function of RNA-binding proteins.

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Metadata

Authors
Liu, Q., & Dreyfuss, G.
Venue
Molecular and Cellular Biology
Published
1995-05-01
Volume
15
Issue
5
Pages
2800-2808
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
OpenAlex
W2151960388
Cited by
305
References
0
FWCI
3.20
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: In Vivo and In Vitro Arginine Methylation of RNA-Binding Proteins. https://app.cochat.ai/papers/10.1128/mcb.15.5.2800
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Liu, Q., & Dreyfuss, G. (1995). In Vivo and In Vitro Arginine Methylation of RNA-Binding Proteins. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.15.5.2800

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