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Arginine methylation of ribosomal protein S3 affects ribosome assembly

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dc.contributor.authorShin, Hyun-Seock-
dc.contributor.authorJang, Chang-Young-
dc.contributor.authorKim, Hag Dong-
dc.contributor.authorKim, Tae-Sung-
dc.contributor.authorKim, Sangduk-
dc.contributor.authorKim, Joon-
dc.date.accessioned2021-09-08T15:26:24Z-
dc.date.available2021-09-08T15:26:24Z-
dc.date.created2021-06-10-
dc.date.issued2009-07-24-
dc.identifier.issn0006-291X-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/119652-
dc.description.abstractThe 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.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherACADEMIC PRESS INC ELSEVIER SCIENCE-
dc.subjectDNA-REPAIR-
dc.subjectMETHYLTRANSFERASES-
dc.subjectCOMPLEX-
dc.subjectBINDING-
dc.subjectRPS3-
dc.subjectERK-
dc.titleArginine methylation of ribosomal protein S3 affects ribosome assembly-
dc.typeArticle-
dc.contributor.affiliatedAuthorShin, Hyun-Seock-
dc.contributor.affiliatedAuthorKim, Tae-Sung-
dc.contributor.affiliatedAuthorKim, Joon-
dc.identifier.doi10.1016/j.bbrc.2009.05.055-
dc.identifier.scopusid2-s2.0-67349234069-
dc.identifier.wosid000267037300028-
dc.identifier.bibliographicCitationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.385, no.2, pp.273 - 278-
dc.relation.isPartOfBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.citation.titleBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.citation.volume385-
dc.citation.number2-
dc.citation.startPage273-
dc.citation.endPage278-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.subject.keywordPlusDNA-REPAIR-
dc.subject.keywordPlusMETHYLTRANSFERASES-
dc.subject.keywordPlusCOMPLEX-
dc.subject.keywordPlusBINDING-
dc.subject.keywordPlusRPS3-
dc.subject.keywordPlusERK-
dc.subject.keywordAuthorRibosomal protein S3 (rpS3)-
dc.subject.keywordAuthorArginine methylation-
dc.subject.keywordAuthorRibosome assembly-
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