Arginine methylation of ribosomal protein S3 affects ribosome assembly.
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.
Shin
Hyun-Seock
HS
Laboratory of Biochemistry, School of Life Sciences & Biotechnology, and BioInstitute, Korea University, Seoul, Republic of Korea.
Jang
Chang-Young
CY
Kim
Hag Dong
HD
Kim
Tae-Sung
TS
Kim
Sangduk
S
Kim
Joon
J
D021581:Active Transport, Cell Nucleus; D000595:Amino Acid Sequence; D001120:Arginine / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D002466:Cell Nucleolus / Q000378:metabolism; D006801:Humans; D008745:Methylation; D011484:Protein-Arginine N-Methyltransferases / Q000378:metabolism; D012097:Repressor Proteins / Q000378:metabolism; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
D012097:Repressor Proteins; D012269:Ribosomal Proteins; C044152:ribosomal protein S3; D001120:Arginine; C099988:PRMT1 protein, human; D011484:Protein-Arginine N-Methyltransferases