Xmas-2 Protein, the Core Protein of the TREX-2 mRNA Export Complex, Does not Determine the Specificity of ras2 mRNA Binding by the Complex

IF 0.8 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY Doklady Biochemistry and Biophysics Pub Date : 2024-08-28 DOI:10.1134/S1607672924600519
M. M. Kurshakova, Y. A. Vdovina,  S. G. Georgieva, D. V. Kopytova
{"title":"Xmas-2 Protein, the Core Protein of the TREX-2 mRNA Export Complex, Does not Determine the Specificity of ras2 mRNA Binding by the Complex","authors":"M. M. Kurshakova,&nbsp;Y. A. Vdovina,&nbsp; S. G. Georgieva,&nbsp;D. V. Kopytova","doi":"10.1134/S1607672924600519","DOIUrl":null,"url":null,"abstract":"<p>The TREX-2 complex of eukaryotes is responsible for the export of a wide range of mRNAs from the nucleus to the cytoplasm. Previously, we showed that a subunit of the <i>D. melanogaster</i> TREX-2 complex, the PCID2 protein, has a domain that specifically interacts with RNA. However, it remains unknown whether other components of the complex are involved in interaction with and recognition of the target mRNA. In the present study, we determined the role of Xmas-2, the core structural subunit of the complex, in the specific recognition of <i>ras2</i> mRNA fragments. In this work, we showed that Xmas-2 interacts with <i>ras2</i> mRNA independently of other subunits of the complex. We showed that RNA-binding domains are located in both the N-terminal domain and the C-terminal domain of Xmas-2. However, the interaction of the protein with <i>ras2</i> mRNA fragments is independent of RNA sequence and structure and is nonspecific. Thus, the Xmas-2 subunit is not involved in the recognition of specific RNA sequences by the complex.</p>","PeriodicalId":529,"journal":{"name":"Doklady Biochemistry and Biophysics","volume":null,"pages":null},"PeriodicalIF":0.8000,"publicationDate":"2024-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Doklady Biochemistry and Biophysics","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1134/S1607672924600519","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

The TREX-2 complex of eukaryotes is responsible for the export of a wide range of mRNAs from the nucleus to the cytoplasm. Previously, we showed that a subunit of the D. melanogaster TREX-2 complex, the PCID2 protein, has a domain that specifically interacts with RNA. However, it remains unknown whether other components of the complex are involved in interaction with and recognition of the target mRNA. In the present study, we determined the role of Xmas-2, the core structural subunit of the complex, in the specific recognition of ras2 mRNA fragments. In this work, we showed that Xmas-2 interacts with ras2 mRNA independently of other subunits of the complex. We showed that RNA-binding domains are located in both the N-terminal domain and the C-terminal domain of Xmas-2. However, the interaction of the protein with ras2 mRNA fragments is independent of RNA sequence and structure and is nonspecific. Thus, the Xmas-2 subunit is not involved in the recognition of specific RNA sequences by the complex.

Abstract Image

Abstract Image

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
TREX-2 mRNA导出复合体的核心蛋白 Xmas-2 蛋白并不决定该复合体与 ras2 mRNA 结合的特异性。
真核生物的 TREX-2 复合物负责将多种 mRNA 从细胞核输出到细胞质。此前,我们曾发现黑腹蝇 TREX-2 复合物的一个亚基--PCID2 蛋白--具有一个能与 RNA 特异性相互作用的结构域。然而,该复合体的其他成分是否参与了与目标 mRNA 的相互作用和识别,目前仍不得而知。在本研究中,我们确定了该复合体的核心结构亚基 Xmas-2 在特异性识别 ras2 mRNA 片段中的作用。在这项工作中,我们发现 Xmas-2 与 ras2 mRNA 的相互作用独立于复合体的其他亚基。我们发现 RNA 结合结构域位于 Xmas-2 的 N 端结构域和 C 端结构域。然而,该蛋白与 ras2 mRNA 片段的相互作用与 RNA 序列和结构无关,而且是非特异性的。因此,Xmas-2 亚基并不参与复合体对特定 RNA 序列的识别。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Doklady Biochemistry and Biophysics
Doklady Biochemistry and Biophysics 生物-生化与分子生物学
CiteScore
1.60
自引率
12.50%
发文量
68
审稿时长
6-12 weeks
期刊介绍: Doklady Biochemistry and Biophysics is a journal consisting of English translations of articles published in Russian in biochemistry and biophysics sections of the Russian-language journal Doklady Akademii Nauk. The journal''s goal is to publish the most significant new research in biochemistry and biophysics carried out in Russia today or in collaboration with Russian authors. The journal accepts only articles in the Russian language that are submitted or recommended by acting Russian or foreign members of the Russian Academy of Sciences. The journal does not accept direct submissions in English.
期刊最新文献
Transriptome Analysis of Peripheral Blood Monocytes in Chronic Obstructive Pulmonary Disease Patients. A Study of the Comparability of the Pharmacodynamic, Toxicological, and Pharmacokinetic Properties of the Reference Drug Pulmozyme® and the Biosimilar Drug Tigerase®. Effect of Bioplastic Material on Adhesion, Growth, and Proliferative Activity of Human Fibroblasts When Incubated in Solutions Mimic the Acidity of Wound an Acute and Chronic Inflammation. Effects of Overexpression of Specific Subunits SAYP, BAP170 of the Chromatin Remodeling Complex in Drosophila Melanogaster. Features of Brain Damage after Neutron Irradiation of the Head and Modification of the Damage by Lactoferrin.
×
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