Arginine methylation of ribosomal protein S3 affects ribosome assembly
- Authors
- Shin, Hyun-Seock; Jang, Chang-Young; Kim, Hag Dong; Kim, Tae-Sung; Kim, Sangduk; Kim, Joon
- Issue Date
- 24-7월-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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