P190A RhoGAP 的 FF1 结构域在 5 M 和 8 M 尿素中的 1H、15N 和 13C 骨架共振赋值。

IF 0.8 4区生物学 Q4 BIOPHYSICS Biomolecular NMR Assignments Pub Date : 2024-10-14 DOI:10.1007/s12104-024-10197-z

Aarão Camilo-Ramos, Dmitry M. Korzhnev, Ramon Pinheiro-Aguiar, Fabio C. L. Almeida

{"title":"P190A RhoGAP 的 FF1 结构域在 5 M 和 8 M 尿素中的 1H、15N 和 13C 骨架共振赋值。","authors":"Aarão Camilo-Ramos, Dmitry M. Korzhnev, Ramon Pinheiro-Aguiar, Fabio C. L. Almeida","doi":"10.1007/s12104-024-10197-z","DOIUrl":null,"url":null,"abstract":"<div><p>The Rho GTPase (Ras homolog GTPases) system is a crucial signal transducer that regulates various cellular processes, including cell cycle and migration, genetic transcription, and apoptosis. In this study, we investigated the unfolded state of the first FF domain (FF1) of P190A RhoGAP, which features four tandem FF domains. For signal transduction, FF1 is phosphorylated at tyrosine 308 (Y308), which is buried in the hydrophobic core and is inaccessible to kinases in the folded domain. It was proposed, therefore, that the phosphorylation occurs in a transiently populated unfolded state of FF1. To probe the folding pathway of the RhoGAP FF1 domain, here we have performed a nearly complete backbone resonance assignments of a putative partially unfolded state of FF1 in 5 M urea and its fully unfolded state in 8 M urea.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"18 2","pages":"257 - 262"},"PeriodicalIF":0.8000,"publicationDate":"2024-10-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Backbone 1H, 15N, and 13C resonance assignments of the FF1 domain from P190A RhoGAP in 5 and 8 M urea\",\"authors\":\"Aarão Camilo-Ramos, Dmitry M. Korzhnev, Ramon Pinheiro-Aguiar, Fabio C. L. Almeida\",\"doi\":\"10.1007/s12104-024-10197-z\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The Rho GTPase (Ras homolog GTPases) system is a crucial signal transducer that regulates various cellular processes, including cell cycle and migration, genetic transcription, and apoptosis. In this study, we investigated the unfolded state of the first FF domain (FF1) of P190A RhoGAP, which features four tandem FF domains. For signal transduction, FF1 is phosphorylated at tyrosine 308 (Y308), which is buried in the hydrophobic core and is inaccessible to kinases in the folded domain. It was proposed, therefore, that the phosphorylation occurs in a transiently populated unfolded state of FF1. To probe the folding pathway of the RhoGAP FF1 domain, here we have performed a nearly complete backbone resonance assignments of a putative partially unfolded state of FF1 in 5 M urea and its fully unfolded state in 8 M urea.</p></div>\",\"PeriodicalId\":492,\"journal\":{\"name\":\"Biomolecular NMR Assignments\",\"volume\":\"18 2\",\"pages\":\"257 - 262\"},\"PeriodicalIF\":0.8000,\"publicationDate\":\"2024-10-14\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biomolecular NMR Assignments\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s12104-024-10197-z\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOPHYSICS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomolecular NMR Assignments","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s12104-024-10197-z","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOPHYSICS","Score":null,"Total":0}

引用次数: 0

摘要

Rho GTPase（Ras 同源物 GTPases）系统是一个重要的信号转导子，它调控各种细胞过程，包括细胞周期和迁移、基因转录和细胞凋亡。在这项研究中，我们研究了 P190A RhoGAP 的第一个 FF 结构域（FF1）的展开状态，该结构域具有四个串联的 FF 结构域。在信号转导过程中，FF1 在酪氨酸 308（Y308）处被磷酸化，该处被埋藏在疏水核心中，折叠结构域中的激酶无法进入。因此，有人提出，磷酸化发生在 FF1 瞬时填充的未折叠状态。为了探究 RhoGAP FF1 结构域的折叠途径，我们对 FF1 在 5 M 尿素中的部分未折叠状态和在 8 M 尿素中的完全未折叠状态进行了近乎完整的骨架共振分析。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

Backbone 1H, 15N, and 13C resonance assignments of the FF1 domain from P190A RhoGAP in 5 and 8 M urea

The Rho GTPase (Ras homolog GTPases) system is a crucial signal transducer that regulates various cellular processes, including cell cycle and migration, genetic transcription, and apoptosis. In this study, we investigated the unfolded state of the first FF domain (FF1) of P190A RhoGAP, which features four tandem FF domains. For signal transduction, FF1 is phosphorylated at tyrosine 308 (Y308), which is buried in the hydrophobic core and is inaccessible to kinases in the folded domain. It was proposed, therefore, that the phosphorylation occurs in a transiently populated unfolded state of FF1. To probe the folding pathway of the RhoGAP FF1 domain, here we have performed a nearly complete backbone resonance assignments of a putative partially unfolded state of FF1 in 5 M urea and its fully unfolded state in 8 M urea.

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

Biomolecular NMR Assignments 生物-光谱学

CiteScore

1.70

自引率

11.10%

发文量

审稿时长

6-12 weeks

期刊介绍： Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.