YgfY Contributes to Stress Tolerance in <i>Shewanella oneidensis</i> Neither as an Antitoxin Nor as a Flavinylation Factor of Succinate Dehydrogenase

YgfY(SdhE/CptB) is highly conserved while has controversial functions in bacteria. It works as an antitoxin and composes a type IV toxin–antitoxin system with YgfX(CptA) typically in <i>Escherichia coli</i>, while functions as an flavinylation factor of succinate dehydrogenase and fumara...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Ming-Xing Zhang, Kai-Li Zheng, Ai-Guo Tang, Xiao-Xia Hu, Xin-Xin Guo, Chao Wu, Yuan-Yuan Cheng
Formato: article
Lenguaje:EN
Publicado: MDPI AG 2021
Materias:
Acceso en línea:https://doaj.org/article/abc70ead58b84d909a3d7599f8350147
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:abc70ead58b84d909a3d7599f8350147
record_format dspace
spelling oai:doaj.org-article:abc70ead58b84d909a3d7599f83501472021-11-25T18:25:04ZYgfY Contributes to Stress Tolerance in <i>Shewanella oneidensis</i> Neither as an Antitoxin Nor as a Flavinylation Factor of Succinate Dehydrogenase10.3390/microorganisms91123162076-2607https://doaj.org/article/abc70ead58b84d909a3d7599f83501472021-11-01T00:00:00Zhttps://www.mdpi.com/2076-2607/9/11/2316https://doaj.org/toc/2076-2607YgfY(SdhE/CptB) is highly conserved while has controversial functions in bacteria. It works as an antitoxin and composes a type IV toxin–antitoxin system with YgfX(CptA) typically in <i>Escherichia coli</i>, while functions as an flavinylation factor of succinate dehydrogenase and fumarate reductase typically in <i>Serratia</i> sp. In this study, we report the contribution of YgfY in <i>Shewanella oneidensis</i> MR-1 to tolerance of low temperature and nitrite. YgfY deficiency causes several growth defects of <i>S. oneidensis</i> MR-1 at low temperature, while YgfX do not cause a growth defect or morphological change of <i>S. oneidensis</i> MR1-1 and <i>E. coli</i>. YgfY do not interact with FtsZ and MreB nor with YgfX examined by bacterial two-hybrid assay. YgfY effect on growth under low temperature is not attributed to succinate dehydrogenase (SDH) because a mutant without SDH grows comparably with the wild-type strain in the presence of succinate. The <i>ygfY</i> mutant shows impaired tolerance to nitrite. Transcription of nitrite reductase and most ribosome proteins is significantly decreased in the <i>ygfY</i> mutant, which is consistent with the phenotypes detected above. Effects of YgfY on growth and nitrite tolerance are closely related to the RGXXE motif in YgfY. In summary, this study demonstrates pleiotropic impacts of YgfY in <i>S. oneidensis</i> MR-1, and sheds a light on the physiological versatility of YgfY in bacteria.Ming-Xing ZhangKai-Li ZhengAi-Guo TangXiao-Xia HuXin-Xin GuoChao WuYuan-Yuan ChengMDPI AGarticleYgfY<i>Shewanella</i>toxin–antitoxinsuccinate dehydrogenaseflavinylationBiology (General)QH301-705.5ENMicroorganisms, Vol 9, Iss 2316, p 2316 (2021)
institution DOAJ
collection DOAJ
language EN
topic YgfY
<i>Shewanella</i>
toxin–antitoxin
succinate dehydrogenase
flavinylation
Biology (General)
QH301-705.5
spellingShingle YgfY
<i>Shewanella</i>
toxin–antitoxin
succinate dehydrogenase
flavinylation
Biology (General)
QH301-705.5
Ming-Xing Zhang
Kai-Li Zheng
Ai-Guo Tang
Xiao-Xia Hu
Xin-Xin Guo
Chao Wu
Yuan-Yuan Cheng
YgfY Contributes to Stress Tolerance in <i>Shewanella oneidensis</i> Neither as an Antitoxin Nor as a Flavinylation Factor of Succinate Dehydrogenase
description YgfY(SdhE/CptB) is highly conserved while has controversial functions in bacteria. It works as an antitoxin and composes a type IV toxin–antitoxin system with YgfX(CptA) typically in <i>Escherichia coli</i>, while functions as an flavinylation factor of succinate dehydrogenase and fumarate reductase typically in <i>Serratia</i> sp. In this study, we report the contribution of YgfY in <i>Shewanella oneidensis</i> MR-1 to tolerance of low temperature and nitrite. YgfY deficiency causes several growth defects of <i>S. oneidensis</i> MR-1 at low temperature, while YgfX do not cause a growth defect or morphological change of <i>S. oneidensis</i> MR1-1 and <i>E. coli</i>. YgfY do not interact with FtsZ and MreB nor with YgfX examined by bacterial two-hybrid assay. YgfY effect on growth under low temperature is not attributed to succinate dehydrogenase (SDH) because a mutant without SDH grows comparably with the wild-type strain in the presence of succinate. The <i>ygfY</i> mutant shows impaired tolerance to nitrite. Transcription of nitrite reductase and most ribosome proteins is significantly decreased in the <i>ygfY</i> mutant, which is consistent with the phenotypes detected above. Effects of YgfY on growth and nitrite tolerance are closely related to the RGXXE motif in YgfY. In summary, this study demonstrates pleiotropic impacts of YgfY in <i>S. oneidensis</i> MR-1, and sheds a light on the physiological versatility of YgfY in bacteria.
format article
author Ming-Xing Zhang
Kai-Li Zheng
Ai-Guo Tang
Xiao-Xia Hu
Xin-Xin Guo
Chao Wu
Yuan-Yuan Cheng
author_facet Ming-Xing Zhang
Kai-Li Zheng
Ai-Guo Tang
Xiao-Xia Hu
Xin-Xin Guo
Chao Wu
Yuan-Yuan Cheng
author_sort Ming-Xing Zhang
title YgfY Contributes to Stress Tolerance in <i>Shewanella oneidensis</i> Neither as an Antitoxin Nor as a Flavinylation Factor of Succinate Dehydrogenase
title_short YgfY Contributes to Stress Tolerance in <i>Shewanella oneidensis</i> Neither as an Antitoxin Nor as a Flavinylation Factor of Succinate Dehydrogenase
title_full YgfY Contributes to Stress Tolerance in <i>Shewanella oneidensis</i> Neither as an Antitoxin Nor as a Flavinylation Factor of Succinate Dehydrogenase
title_fullStr YgfY Contributes to Stress Tolerance in <i>Shewanella oneidensis</i> Neither as an Antitoxin Nor as a Flavinylation Factor of Succinate Dehydrogenase
title_full_unstemmed YgfY Contributes to Stress Tolerance in <i>Shewanella oneidensis</i> Neither as an Antitoxin Nor as a Flavinylation Factor of Succinate Dehydrogenase
title_sort ygfy contributes to stress tolerance in <i>shewanella oneidensis</i> neither as an antitoxin nor as a flavinylation factor of succinate dehydrogenase
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/abc70ead58b84d909a3d7599f8350147
work_keys_str_mv AT mingxingzhang ygfycontributestostresstoleranceinishewanellaoneidensisineitherasanantitoxinnorasaflavinylationfactorofsuccinatedehydrogenase
AT kailizheng ygfycontributestostresstoleranceinishewanellaoneidensisineitherasanantitoxinnorasaflavinylationfactorofsuccinatedehydrogenase
AT aiguotang ygfycontributestostresstoleranceinishewanellaoneidensisineitherasanantitoxinnorasaflavinylationfactorofsuccinatedehydrogenase
AT xiaoxiahu ygfycontributestostresstoleranceinishewanellaoneidensisineitherasanantitoxinnorasaflavinylationfactorofsuccinatedehydrogenase
AT xinxinguo ygfycontributestostresstoleranceinishewanellaoneidensisineitherasanantitoxinnorasaflavinylationfactorofsuccinatedehydrogenase
AT chaowu ygfycontributestostresstoleranceinishewanellaoneidensisineitherasanantitoxinnorasaflavinylationfactorofsuccinatedehydrogenase
AT yuanyuancheng ygfycontributestostresstoleranceinishewanellaoneidensisineitherasanantitoxinnorasaflavinylationfactorofsuccinatedehydrogenase
_version_ 1718411217128652800