Detailed Information

Cited 36 time in webofscience Cited 38 time in scopus
Metadata Downloads

Arginine methylation of ribosomal protein S3 affects ribosome assembly

Authors
Shin, Hyun-SeockJang, Chang-YoungKim, Hag DongKim, Tae-SungKim, SangdukKim, Joon
Issue Date
24-Jul-2009
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
Ribosomal protein S3 (rpS3); Arginine methylation; Ribosome assembly
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.385, no.2, pp 273 - 278
Pages
6
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
385
Number
2
Start Page
273
End Page
278
URI
https://scholarworks.korea.ac.kr/kumedicine/handle/2020.sw.kumedicine/15893
DOI
10.1016/j.bbrc.2009.05.055
ISSN
0006-291X
1090-2104
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. (C) 2009 Elsevier Inc. All rights reserved.
Files in This Item
There are no files associated with this item.
Appears in
Collections
4. Research institute > Cancer Institute > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Related Researcher

Researcher Shin, Hyun Seock photo

Shin, Hyun Seock
Research Institute (Cancer Institute)
Read more

Altmetrics

Total Views & Downloads

BROWSE