Arginine methylation of ribosomal protein S3 affects ribosome assembly

Hyun Seock Shin, Chang Young Jang, Hag Dong Kim, Tae Sung Kim, Sangduk Kim, Joon Kim

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

The human ribosomal protein S3 (rpS3), a component of the 40S small subunit in the ribosome, is a known multi-functional protein with roles in DNA repair and apoptosis. We recently found that the arginine residue(s) of rpS3 are methylated by protein arginine methyltransferase 1 (PRMT1). In this paper, we confirmed the arginine methylation of rpS3 protein both in vitro and in vivo. The sites of arginine methylation are located at amino acids 64, 65 and 67. However, mutant rpS3 (3RA), which cannot be methylated at these sites, cannot be transported into the nucleolus and subsequently incorporated into the ribosome. Our results clearly show that arginine methylation of rpS3 plays a critical role in its import into the nucleolus, as well as in small subunit assembly of the ribosome.

Original languageEnglish
Pages (from-to)273-278
Number of pages6
JournalBiochemical and biophysical research communications
Volume385
Issue number2
DOIs
Publication statusPublished - 2009 Jul 24

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Keywords

  • Arginine methylation
  • Ribosomal protein S3 (rpS3)
  • Ribosome assembly

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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