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Recent advances in protein methylation: Enzymatic methylation of nucleic acid binding proteins

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Summary

Heterogeneous nuclear RNP protein A1, one of the major proteins in hnRNP particle (precursor for mRNA), is known to be post-translationally arginine-methylatedin vivo on residues 193, 205, 217 and 224 within the RGG box, the motif postulated to be an RNA binding domain. Possible effect of NG-arginine methyl-modification in the interaction of protein A1 to nucleic acid was investigated. The recombinant hnRNP protein A1 wasin vitro methylated by the purified nuclear protein/histone-specific protein methylase I (S-adenosylmethionine:protein-arginine N-methyltransferase) stoichiometrically and the relative binding affinity of the methylated and the unmethylated protein A1 to nucleic acid was compared: Differences in their binding properties to ssDNA-cellulose, pI values and trypsin sensitivities in the presence and absence of MS2-RNA all indicate that the binding property of hnRNP protein A1 to single-stranded nucleic acid has been significantly reduced subsequent to the methylation. These results suggest that posttranslational methyl group insertion to the arginine residue reduces protein-RNA interaction, perhaps due to interference of H-bonding between guanidino nitrogen arginine and phosphate RNA.

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Abbreviations

hnRNP:

heterogeneous ribonucleoprotein particle

AdoMet:

S-adenosyl-L-methionine

AdoHcy:

S-adenosyl-L-homocysteine

MBP:

myelin basic protein

HMG:

high mobility group

ss:

single stranded

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Authors and Affiliations

  1. Department of Biochemistry, Korea University Medical School, 126, 5-Ga Anam-Dong, 136-701, Sung Buk-Gu, Seoul, Korea

    Sangduk Kim & G. H. Park

  2. Department of Biochemistry, School of Medicine, Ajou University, Suwon, Korea

    W. K. Paik

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  1. Sangduk Kim
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  2. G. H. Park
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  3. W. K. Paik
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Kim, S., Park, G.H. & Paik, W.K. Recent advances in protein methylation: Enzymatic methylation of nucleic acid binding proteins. Amino Acids 15, 291–306 (1998). https://doi.org/10.1007/BF01320895

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  • DOI: https://doi.org/10.1007/BF01320895

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