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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
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
385
Number
2
Start Page
273
End Page
278
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/119652
DOI
10.1016/j.bbrc.2009.05.055
ISSN
0006-291X
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.
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