Regulation of post-translational protein arginine methylation during HeLa cell cycle
DC Field | Value | Language |
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dc.contributor.author | Kim, Chongtae | - |
dc.contributor.author | Lim, Yongchul | - |
dc.contributor.author | Yoo, Byong Chul | - |
dc.contributor.author | Won, Nam Hee | - |
dc.contributor.author | Kim, Sangduk | - |
dc.contributor.author | Kim, Gieun | - |
dc.date.accessioned | 2021-09-08T00:41:56Z | - |
dc.date.available | 2021-09-08T00:41:56Z | - |
dc.date.created | 2021-06-14 | - |
dc.date.issued | 2010-09 | - |
dc.identifier.issn | 0304-4165 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/115825 | - |
dc.description.abstract | Background: Post-translational arginine methylation which modifies protein-arginyl residues by protein arginine methyltransferase (PRMT) was investigated during synchronized HeLa cell cycle. Methods: The lysates of cells synchronized at each stage were subjected to one and/or two dimensional electrophoresis followed by Western immunoblot using against anti-asymmetric-dimethyl-arginine (ASYM24), anti-symmetric-dimethyl-arginine (SYM10), and subclasses of PRMTs, including PRMT1, PRMT3, PRMT4 (CARM1), PRMT5, PRMT6, and PRMT7 antibodies. Results: Proteins with approximate molecular masses of 80 kDa, 68 kDa, and 64 kDa, containing asymmetric-dimethyl-arginine (aDMA) were increased at G0/G1 to G1, which lasted until S phase. In addition. 25 kDa protein of symmetric-dimethyl-arginine (sDMA) was also markedly up-regulated from G0/G1 to G1. The levels of PRMT3, PRMT6 and PRMT7 were concurrently increased during the cell cycle. Two-dimensional gel electrophoresis followed by MALDI-TOF-MS was identified as aDMA-80 kDa and aDMA-68 kDa proteins as heterogeneous nuclear ribonucleoprotein R (hnRNPR), aDMA-64 kDa proteins as cleavage stimulation factor 64 kDa subunit (CstF-64), and sDMA-25 kDa protein as triosephosphate isomerase (TPI). The levels of increased aDMA of hnRNPR were reduced, when HeLa cells were transfected with siRNA for PRMT1, and the aDMA of CstF-64 with siRNA for PRMT3, while depletion of PRMT5 down-regulated sDMA of TPI. Conclusion: Protein arginine dimethylations of hnRNPR, CstF-64, and TPI were regulated during HeLa cell cycle by respective PRMTs. General significance: These results suggest that regulation of arginine dimethylation of hnRNPR, CstF-64, and TPI at G0/G1 to G1 are most likely to modulate the cellular growth and proliferation in HeLa cell cycle. (C) 2010 Elsevier B.V. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN | - |
dc.subject | TRIOSEPHOSPHATE ISOMERASE | - |
dc.subject | N-METHYLTRANSFERASE | - |
dc.subject | IN-VITRO | - |
dc.subject | BINDING | - |
dc.subject | EXPRESSION | - |
dc.subject | MOUSE | - |
dc.subject | PRMT1 | - |
dc.subject | IDENTIFICATION | - |
dc.subject | RESIDUES | - |
dc.title | Regulation of post-translational protein arginine methylation during HeLa cell cycle | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Won, Nam Hee | - |
dc.contributor.affiliatedAuthor | Kim, Sangduk | - |
dc.identifier.doi | 10.1016/j.bbagen.2010.06.004 | - |
dc.identifier.scopusid | 2-s2.0-77955272369 | - |
dc.identifier.wosid | 000281182800010 | - |
dc.identifier.bibliographicCitation | BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, v.1800, no.9, pp.977 - 985 | - |
dc.relation.isPartOf | BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | - |
dc.citation.title | BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | - |
dc.citation.volume | 1800 | - |
dc.citation.number | 9 | - |
dc.citation.startPage | 977 | - |
dc.citation.endPage | 985 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN | - |
dc.subject.keywordPlus | TRIOSEPHOSPHATE ISOMERASE | - |
dc.subject.keywordPlus | N-METHYLTRANSFERASE | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | MOUSE | - |
dc.subject.keywordPlus | PRMT1 | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | RESIDUES | - |
dc.subject.keywordAuthor | omega-N-G,N-G-asymmetric and omega-N-G,N &apos | - |
dc.subject.keywordAuthor | (G)-symmetric dimethyl-arginine | - |
dc.subject.keywordAuthor | Hela cell cycle | - |
dc.subject.keywordAuthor | Protein arginine methyltransferases | - |
dc.subject.keywordAuthor | Heterogeneous nuclear ribonucleoprotein R | - |
dc.subject.keywordAuthor | Cleavage stimulation factor 64 kDa subunit | - |
dc.subject.keywordAuthor | Triosephosphate isomerase | - |
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