在大肠杆菌中,核糖核苷酸单磷酸酶 UmpH 的活性受控于与 GlnK 信号蛋白的相互作用。

IF 4 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Ana Carolina Aparecida Gonçalves, Tatiana de Mello Damasco Nunes, Erick Parize, Edileusa Cristina Marques Gerhardt, Gustavo Antônio de Souza, Jörg Scholl, Karl Forchhammer, Luciano Fernandes Huergo
{"title":"在大肠杆菌中,核糖核苷酸单磷酸酶 UmpH 的活性受控于与 GlnK 信号蛋白的相互作用。","authors":"Ana Carolina Aparecida Gonçalves, Tatiana de Mello Damasco Nunes, Erick Parize, Edileusa Cristina Marques Gerhardt, Gustavo Antônio de Souza, Jörg Scholl, Karl Forchhammer, Luciano Fernandes Huergo","doi":"10.1016/j.jbc.2024.107931","DOIUrl":null,"url":null,"abstract":"<p><p>The PII signaling proteins are ubiquitous in prokaryotes serving as crucial metabolic hubs in different metabolic pathways due to their ability to sense and integrate signals of the cellular nitrogen, carbon, and energy levels. In this study we used ligand fishing assays to identify the ribonucleotide monophosphatase UmpH enzyme as a novel target of the PII signaling protein GlnK in Escherichia coli. In vitro analyses showed that UmpH interacts specifically with the PII protein GlnK but not with its paralogue protein GlnB. The UmpH - GlnK complex is modulated by the GlnK uridylylation status and by the levels of the GlnK allosteric effectors ATP, ADP and 2-oxoglutarate. Upon engaging interaction with GlnK, UmpH becomes less active towards its substrate uridine 5'-monophosphate (UMP). We suggest a model where GlnK will physically interact to reduce the UmpH activity during the transition from N-starvation to N-sufficient conditions. Such a mechanism may help the cells to reprogram the fate of UMP from catabolism to anabolism avoiding futile cycling of key nutrients.</p>","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":null,"pages":null},"PeriodicalIF":4.0000,"publicationDate":"2024-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The activity of the ribonucleotide monophosphatase UmpH is controlled by interaction with the GlnK signaling protein in Escherichia coli.\",\"authors\":\"Ana Carolina Aparecida Gonçalves, Tatiana de Mello Damasco Nunes, Erick Parize, Edileusa Cristina Marques Gerhardt, Gustavo Antônio de Souza, Jörg Scholl, Karl Forchhammer, Luciano Fernandes Huergo\",\"doi\":\"10.1016/j.jbc.2024.107931\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The PII signaling proteins are ubiquitous in prokaryotes serving as crucial metabolic hubs in different metabolic pathways due to their ability to sense and integrate signals of the cellular nitrogen, carbon, and energy levels. In this study we used ligand fishing assays to identify the ribonucleotide monophosphatase UmpH enzyme as a novel target of the PII signaling protein GlnK in Escherichia coli. In vitro analyses showed that UmpH interacts specifically with the PII protein GlnK but not with its paralogue protein GlnB. The UmpH - GlnK complex is modulated by the GlnK uridylylation status and by the levels of the GlnK allosteric effectors ATP, ADP and 2-oxoglutarate. Upon engaging interaction with GlnK, UmpH becomes less active towards its substrate uridine 5'-monophosphate (UMP). We suggest a model where GlnK will physically interact to reduce the UmpH activity during the transition from N-starvation to N-sufficient conditions. Such a mechanism may help the cells to reprogram the fate of UMP from catabolism to anabolism avoiding futile cycling of key nutrients.</p>\",\"PeriodicalId\":15140,\"journal\":{\"name\":\"Journal of Biological Chemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.0000,\"publicationDate\":\"2024-10-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Biological Chemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1016/j.jbc.2024.107931\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Biological Chemistry","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1016/j.jbc.2024.107931","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

PII 信号蛋白在原核生物中无处不在,由于它们能够感知和整合细胞氮、碳和能量水平的信号,因此是不同代谢途径中的关键代谢枢纽。在这项研究中,我们利用配体钓取试验确定了核糖核苷酸单磷酸酶 UmpH 酶是大肠杆菌中 PII 信号蛋白 GlnK 的新靶标。体外分析表明,UmpH 与 PII 蛋白 GlnK 有特异性相互作用,但与其同源蛋白 GlnB 没有相互作用。UmpH - GlnK 复合物受 GlnK 尿苷酸化状态以及 GlnK 异生效应物质 ATP、ADP 和 2-oxoglutarate 水平的调节。与 GlnK 相互作用后,UmpH 对其底物尿苷-5'-单磷酸(UMP)的活性降低。我们提出了一个模型,即在从氮饥饿向氮充足条件过渡的过程中,GlnK 将通过物理作用降低 UmpH 的活性。这种机制可能有助于细胞重新规划 UMP 的命运,将其从分解代谢转变为合成代谢,避免关键营养物质的徒劳循环。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The activity of the ribonucleotide monophosphatase UmpH is controlled by interaction with the GlnK signaling protein in Escherichia coli.

The PII signaling proteins are ubiquitous in prokaryotes serving as crucial metabolic hubs in different metabolic pathways due to their ability to sense and integrate signals of the cellular nitrogen, carbon, and energy levels. In this study we used ligand fishing assays to identify the ribonucleotide monophosphatase UmpH enzyme as a novel target of the PII signaling protein GlnK in Escherichia coli. In vitro analyses showed that UmpH interacts specifically with the PII protein GlnK but not with its paralogue protein GlnB. The UmpH - GlnK complex is modulated by the GlnK uridylylation status and by the levels of the GlnK allosteric effectors ATP, ADP and 2-oxoglutarate. Upon engaging interaction with GlnK, UmpH becomes less active towards its substrate uridine 5'-monophosphate (UMP). We suggest a model where GlnK will physically interact to reduce the UmpH activity during the transition from N-starvation to N-sufficient conditions. Such a mechanism may help the cells to reprogram the fate of UMP from catabolism to anabolism avoiding futile cycling of key nutrients.

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
Journal of Biological Chemistry
Journal of Biological Chemistry Biochemistry, Genetics and Molecular Biology-Biochemistry
自引率
4.20%
发文量
1233
期刊介绍: The Journal of Biological Chemistry welcomes high-quality science that seeks to elucidate the molecular and cellular basis of biological processes. Papers published in JBC can therefore fall under the umbrellas of not only biological chemistry, chemical biology, or biochemistry, but also allied disciplines such as biophysics, systems biology, RNA biology, immunology, microbiology, neurobiology, epigenetics, computational biology, ’omics, and many more. The outcome of our focus on papers that contribute novel and important mechanistic insights, rather than on a particular topic area, is that JBC is truly a melting pot for scientists across disciplines. In addition, JBC welcomes papers that describe methods that will help scientists push their biochemical inquiries forward and resources that will be of use to the research community.
×
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