The serine-arginine (SR) protein UmRrm75 from Ustilago maydis is a functional ortholog of yeast ScHrb1.

IF 2.3 4区 生物学 Q3 BIOTECHNOLOGY & APPLIED MICROBIOLOGY
International Microbiology Pub Date : 2024-06-01 Epub Date: 2023-09-30 DOI:10.1007/s10123-023-00432-3
Alma Laura Rodríguez-Piña, Enrique Castaño de la Serna, Juan Francisco Jiménez-Bremont
{"title":"The serine-arginine (SR) protein UmRrm75 from Ustilago maydis is a functional ortholog of yeast ScHrb1.","authors":"Alma Laura Rodríguez-Piña, Enrique Castaño de la Serna, Juan Francisco Jiménez-Bremont","doi":"10.1007/s10123-023-00432-3","DOIUrl":null,"url":null,"abstract":"<p><p>The Basidiomycete fungus Ustilago maydis is a biotrophic pathogen of maize. The U. maydis UmRrm75 gene encodes an RNA-binding protein (RBP). In a previous study, we reported that ΔUmRrm75 null mutant strains accumulate H<sub>2</sub>O<sub>2</sub>, exhibit slow growth, and have decreased virulence in maize. Herein, we describe UmRrm75 as an ortholog of the ScHrb1, a serine-arginine (SR) protein identified in the yeast Saccharomyces cerevisiae, which plays a role in nuclear quality control, specifically in mRNA splicing and export processes. The yeast ScHrb1 mutant (ΔScHrb1) exhibits an increased sensitivity to elevated levels of boron. We noticed that the ΔScHrb1 displayed sensitivity to H<sub>2</sub>O<sub>2</sub>, which is consistent with previous findings in the ΔUmRrm75 mutant. We reversed the sensitivity phenotypes of boron and H<sub>2</sub>O<sub>2</sub> by introducing the UmRrm75 gene into the ΔScHrb1 mutant. Furthermore, we generated complementary strains of U. maydis by expressing UmRrm75-GFP under its native promoter in the ∆UmRrm75 mutants. The UmRrm75-GFP/∆UmRrm75 complementary strains successfully recovered their growth capability under stressors, H<sub>2</sub>O<sub>2</sub> and boron, resembling the parental strains FB2 and AB33. The subcellular localization experiments conducted in U. maydis revealed that the UmRrm75 protein is localized within the nucleus of both yeast and hyphae. The nuclear localization of the UmRrm75 protein remains unaltered even under conditions of heat or oxidative stress. This suggests that UmRrm75 might perform its RBP activity in the nucleus, as previously reported for ScHrb1. Our data contribute to understanding the role of the nuclear RBP UmRrm75 from the corn smut fungus U. maydis.</p>","PeriodicalId":14318,"journal":{"name":"International Microbiology","volume":null,"pages":null},"PeriodicalIF":2.3000,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Microbiology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1007/s10123-023-00432-3","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2023/9/30 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

The Basidiomycete fungus Ustilago maydis is a biotrophic pathogen of maize. The U. maydis UmRrm75 gene encodes an RNA-binding protein (RBP). In a previous study, we reported that ΔUmRrm75 null mutant strains accumulate H2O2, exhibit slow growth, and have decreased virulence in maize. Herein, we describe UmRrm75 as an ortholog of the ScHrb1, a serine-arginine (SR) protein identified in the yeast Saccharomyces cerevisiae, which plays a role in nuclear quality control, specifically in mRNA splicing and export processes. The yeast ScHrb1 mutant (ΔScHrb1) exhibits an increased sensitivity to elevated levels of boron. We noticed that the ΔScHrb1 displayed sensitivity to H2O2, which is consistent with previous findings in the ΔUmRrm75 mutant. We reversed the sensitivity phenotypes of boron and H2O2 by introducing the UmRrm75 gene into the ΔScHrb1 mutant. Furthermore, we generated complementary strains of U. maydis by expressing UmRrm75-GFP under its native promoter in the ∆UmRrm75 mutants. The UmRrm75-GFP/∆UmRrm75 complementary strains successfully recovered their growth capability under stressors, H2O2 and boron, resembling the parental strains FB2 and AB33. The subcellular localization experiments conducted in U. maydis revealed that the UmRrm75 protein is localized within the nucleus of both yeast and hyphae. The nuclear localization of the UmRrm75 protein remains unaltered even under conditions of heat or oxidative stress. This suggests that UmRrm75 might perform its RBP activity in the nucleus, as previously reported for ScHrb1. Our data contribute to understanding the role of the nuclear RBP UmRrm75 from the corn smut fungus U. maydis.

Abstract Image

玉米黑罗非鱼丝氨酸精氨酸(SR)蛋白UmRrm75是酵母ScHrb1的功能同源物。
担子菌是玉米的一种生物营养性病原体。maydis UmRrm75基因编码一种RNA结合蛋白(RBP)。在之前的一项研究中,我们报道了ΔUmRrm75无效突变株在玉米中积累H2O2,表现出缓慢的生长,并降低了毒力。在此,我们将UmRrm75描述为在酿酒酵母中鉴定的丝氨酸精氨酸(SR)蛋白ScHrb1的直系同源物,它在核质量控制中发挥作用,特别是在mRNA剪接和输出过程中。酵母ScHrb1突变体(Δ。我们注意到ΔScHrb1对H2O2表现出敏感性,这与之前在ΔUmRrm75突变体中的发现一致。我们通过将UmRrm75基因引入ΔScHrb1突变体中,逆转了硼和H2O2的敏感性表型。此外,我们通过在∆UmRrm75突变体中在其天然启动子下表达UmRrm75GFP,产生了玉米分枝杆菌的互补菌株。UmRrm75GFP/∆UmRrm75互补菌株在H2O2和硼胁迫下成功恢复了生长能力,类似于亲本菌株FB2和AB33。在玉米中进行的亚细胞定位实验表明,UmRrm75蛋白定位在酵母和菌丝的细胞核内。UmRrm75蛋白的核定位即使在热或氧化应激条件下也保持不变。这表明UmRrm75可能在细胞核中发挥其RBP活性,正如先前报道的ScHrb1一样。我们的数据有助于理解玉米黑穗病真菌U.maydis的核RBP UmRrm75的作用。
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 求助全文
来源期刊
International Microbiology
International Microbiology 生物-生物工程与应用微生物
CiteScore
5.50
自引率
3.20%
发文量
67
审稿时长
3 months
期刊介绍: International Microbiology publishes information on basic and applied microbiology for a worldwide readership. The journal publishes articles and short reviews based on original research, articles about microbiologists and their work and questions related to the history and sociology of this science. Also offered are perspectives, opinion, book reviews and editorials. A distinguishing feature of International Microbiology is its broadening of the term microbiology to include eukaryotic microorganisms.
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信