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

Fingerprint

Methylation
Ribosomes
Arginine
Small Ribosome Subunits
Protein-Arginine N-Methyltransferases
Mutant Proteins
DNA Repair
Proteins
Repair
Apoptosis
Amino Acids
ribosomal protein S3
DNA

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Arginine methylation of ribosomal protein S3 affects ribosome assembly. / Shin, Hyun Seock; Jang, Chang Young; Kim, Hag Dong; Kim, Tae Sung; Kim, Sangduk; Kim, Joon.

In: Biochemical and Biophysical Research Communications, Vol. 385, No. 2, 24.07.2009, p. 273-278.

Research output: Contribution to journalArticle

Shin, Hyun Seock ; Jang, Chang Young ; Kim, Hag Dong ; Kim, Tae Sung ; Kim, Sangduk ; Kim, Joon. / Arginine methylation of ribosomal protein S3 affects ribosome assembly. In: Biochemical and Biophysical Research Communications. 2009 ; Vol. 385, No. 2. pp. 273-278.
@article{c164a96ceda549ab8c5d2420c14e90f3,
title = "Arginine methylation of ribosomal protein S3 affects ribosome assembly",
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.",
keywords = "Arginine methylation, Ribosomal protein S3 (rpS3), Ribosome assembly",
author = "Shin, {Hyun Seock} and Jang, {Chang Young} and Kim, {Hag Dong} and Kim, {Tae Sung} and Sangduk Kim and Joon Kim",
year = "2009",
month = "7",
day = "24",
doi = "10.1016/j.bbrc.2009.05.055",
language = "English",
volume = "385",
pages = "273--278",
journal = "The BMJ",
issn = "0730-6512",
publisher = "Kluwer Academic Publishers",
number = "2",

}

TY - JOUR

T1 - Arginine methylation of ribosomal protein S3 affects ribosome assembly

AU - Shin, Hyun Seock

AU - Jang, Chang Young

AU - Kim, Hag Dong

AU - Kim, Tae Sung

AU - Kim, Sangduk

AU - Kim, Joon

PY - 2009/7/24

Y1 - 2009/7/24

N2 - 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.

AB - 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.

KW - Arginine methylation

KW - Ribosomal protein S3 (rpS3)

KW - Ribosome assembly

UR - http://www.scopus.com/inward/record.url?scp=67349234069&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=67349234069&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2009.05.055

DO - 10.1016/j.bbrc.2009.05.055

M3 - Article

C2 - 19460357

AN - SCOPUS:67349234069

VL - 385

SP - 273

EP - 278

JO - The BMJ

JF - The BMJ

SN - 0730-6512

IS - 2

ER -