Identification of the methylation preference region in heterogeneous nuclear ribonucleoprotein K by protein arginine methyltransferase 1 and its implication in regulating nuclear/cytoplasmic distribution

Yuan I. Chang, Sheng Chieh Hsu, Gar Yang Chau, Chi Ying F. Huang, Jung Sung Sung, Wei Kai Hua, Wey Jinq Lin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

Protein arginine methylation plays crucial roles in numerous cellular processes. Heterogeneous nuclear ribonucleoprotein K (hnRNP K) is a multi-functional protein participating in a variety of cellular functions including transcription and RNA processing. HnRNP K is methylated at multiple sites in the glycine- and arginine-rich (RGG) motif. Using various RGG domain deletion mutants of hnRNP K as substrates, here we show by direct methylation assay that protein arginine methyltransferase 1 (PRMT1) methylated preferentially in a.a. 280-307 of the RGG motif. Kinetic analysis revealed that deletion of a.a. 280-307, but not a.a. 308-327, significantly inhibited rate of methylation. Importantly, nuclear localization of hnRNP K was significantly impaired in mutant hnRNP K lacking the PRMT1 methylation region or upon pharmacological inhibition of methylation. Together our results identify preferred PRMT1 methylation sequences of hnRNP K by direct methylation assay and implicate a role of arginine methylation in regulating intracellular distribution of hnRNP K.

Original languageEnglish
Pages (from-to)865-869
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume404
Issue number3
DOIs
StatePublished - 21 Jan 2011

Keywords

  • Cytoplasmic/nuclear distribution
  • Heterogeneous nuclear ribonucleoprotein K
  • Protein arginine methylation
  • Protein arginine methyltransferase 1

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