[用GST下拉法鉴定HeLa细胞中人核仁蛋白SURF6的蛋白伴侣]。

Bioorganicheskaia khimiia Pub Date : 2014-07-01
M Iu Kordiukova, M A Polzikov, K V Shishova, O V Zatsepina
{"title":"[用GST下拉法鉴定HeLa细胞中人核仁蛋白SURF6的蛋白伴侣]。","authors":"M Iu Kordiukova,&nbsp;M A Polzikov,&nbsp;K V Shishova,&nbsp;O V Zatsepina","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The eukaryotic proteins comprising the SURF6 protein family are evolutionary conservative and housekeeping proteins however, functional roles of human SURF6 have not been studied so far. To shed light to this question in the present work we applied GST pull-down assay and used two proteins fused with GST, namely human GST-SURF6 and the conservative C-terminal domain of mouse Surf6 that has 85% homology with the C-terminus of the human SURF6 conservative domain (GST-Surf6-dom), to identify SURF6-interacting proteins in human HeLa cells. The results obtained showed that GST-SURF6 interacts with several key nucleolar RNA processing factors (B23/nucleophosmin, nucleolin, EBP2), and also with the specific cofactor of RNA polymerase I, protein UBE These results are the first experimental evidences in favor of participation of the human SURF6 protein in ribosome biogenesis, including transcription of rDNA and processing of rRNAs. The same results were obtained, when GST-Surf6-dom was used to pull-down proteins in HeLa cells. In addition, the panel of the GST-Surf6-dom protein partners, which were identified by mass-spectrometry, points to putative interactions of human SURF6 with a number of nuclear and nucleolar, proteins of other functional groups, i.e. to the protein plurifunctionality.</p>","PeriodicalId":9325,"journal":{"name":"Bioorganicheskaia khimiia","volume":"40 4","pages":"421-32"},"PeriodicalIF":0.0000,"publicationDate":"2014-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Identification of the protein partners of the human nucleolar protein SURF6 in HeLa cells by GST pull-down assay].\",\"authors\":\"M Iu Kordiukova,&nbsp;M A Polzikov,&nbsp;K V Shishova,&nbsp;O V Zatsepina\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The eukaryotic proteins comprising the SURF6 protein family are evolutionary conservative and housekeeping proteins however, functional roles of human SURF6 have not been studied so far. To shed light to this question in the present work we applied GST pull-down assay and used two proteins fused with GST, namely human GST-SURF6 and the conservative C-terminal domain of mouse Surf6 that has 85% homology with the C-terminus of the human SURF6 conservative domain (GST-Surf6-dom), to identify SURF6-interacting proteins in human HeLa cells. The results obtained showed that GST-SURF6 interacts with several key nucleolar RNA processing factors (B23/nucleophosmin, nucleolin, EBP2), and also with the specific cofactor of RNA polymerase I, protein UBE These results are the first experimental evidences in favor of participation of the human SURF6 protein in ribosome biogenesis, including transcription of rDNA and processing of rRNAs. The same results were obtained, when GST-Surf6-dom was used to pull-down proteins in HeLa cells. In addition, the panel of the GST-Surf6-dom protein partners, which were identified by mass-spectrometry, points to putative interactions of human SURF6 with a number of nuclear and nucleolar, proteins of other functional groups, i.e. to the protein plurifunctionality.</p>\",\"PeriodicalId\":9325,\"journal\":{\"name\":\"Bioorganicheskaia khimiia\",\"volume\":\"40 4\",\"pages\":\"421-32\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2014-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioorganicheskaia khimiia\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioorganicheskaia khimiia","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

摘要

包含SURF6蛋白家族的真核蛋白是进化保守和管家蛋白,但迄今为止尚未对人类SURF6的功能作用进行研究。为了阐明这一问题,本研究采用GST下拉法,并利用与GST融合的两种蛋白,即人类GST-Surf6和小鼠Surf6的保守c端结构域(GST-Surf6-dom),与人类Surf6保守结构域的c端具有85%的同源性,来鉴定人类HeLa细胞中Surf6的相互作用蛋白。结果表明,GST-SURF6与几个关键的核仁RNA加工因子(B23/nucleophosmin, nucleolin, EBP2)相互作用,并与RNA聚合酶I特异性辅因子UBE蛋白相互作用,这些结果是支持人类SURF6蛋白参与核糖体生物发生的第一个实验证据,包括rDNA的转录和rrna的加工。当使用GST-Surf6-dom拉下HeLa细胞中的蛋白质时,获得了相同的结果。此外,通过质谱鉴定的GST-Surf6-dom蛋白伴侣组指出,人类SURF6可能与许多其他功能基团的核和核核蛋白相互作用,即蛋白质的多功能性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
[Identification of the protein partners of the human nucleolar protein SURF6 in HeLa cells by GST pull-down assay].

The eukaryotic proteins comprising the SURF6 protein family are evolutionary conservative and housekeeping proteins however, functional roles of human SURF6 have not been studied so far. To shed light to this question in the present work we applied GST pull-down assay and used two proteins fused with GST, namely human GST-SURF6 and the conservative C-terminal domain of mouse Surf6 that has 85% homology with the C-terminus of the human SURF6 conservative domain (GST-Surf6-dom), to identify SURF6-interacting proteins in human HeLa cells. The results obtained showed that GST-SURF6 interacts with several key nucleolar RNA processing factors (B23/nucleophosmin, nucleolin, EBP2), and also with the specific cofactor of RNA polymerase I, protein UBE These results are the first experimental evidences in favor of participation of the human SURF6 protein in ribosome biogenesis, including transcription of rDNA and processing of rRNAs. The same results were obtained, when GST-Surf6-dom was used to pull-down proteins in HeLa cells. In addition, the panel of the GST-Surf6-dom protein partners, which were identified by mass-spectrometry, points to putative interactions of human SURF6 with a number of nuclear and nucleolar, proteins of other functional groups, i.e. to the protein plurifunctionality.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
ONE-POT THREE-COMPONENT MICROWAVE-ASSISTED SYNTHESIS OF NOVEL THIAZOLIDINONE DERIVATIVES CONTAINING THIENO[d]PYRIMIDINE-4-ONE MOIETY AS POTENTIAL ANTIMICROBIAL AGENTS. SYNTHESIS AND BIOLOGICAL EVALUATION OF NOVEL COUMARIN DERIVATIVES AS ANTIOXIDANT AGENTS. SYNTHESIS AND IN VITRO ANTIMICROBIAL EVALUATION OF PIPERAZINE SUBSTITUTED QUINAZOLINE-BASED THIOUREA/THIAZOLIDINONE/CHALCONE HYBRIDS. SYNTHESIS AND BIOLOGICAL EVALUATION OF N-(SUBSTITUTED PHENYL)-2-(5H-[1,2,4]TRIAZINO[5,6-b]INDOL-3-YLSULFANYL)ACETAMIDES AS ANTIMICROBIAL, ANTIDEPRESSANT AND ANTICONVULSANT AGENTS. [Creation and Study of Triterpenoid Nanoparticles and Amphiphilic meso-Arylporphyrins].
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1