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NopD of Bradyrhizobium sp. XS1150 Possesses SUMO Protease Activity
Effectors secreted by the type III protein secretion system (T3SS) of rhizobia are host-specific determinants of the nodule symbiosis. Here, we have characterized NopD, a putative type III effector of Bradyrhizobium sp. XS1150. NopD was found to possess a functional N-terminal secretion signal seque...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7098955/ https://www.ncbi.nlm.nih.gov/pubmed/32265858 http://dx.doi.org/10.3389/fmicb.2020.00386 |
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author | Xiang, Qi-Wang Bai, Juan Cai, Jie Huang, Qin-Ying Wang, Yan Liang, Ying Zhong, Zhi Wagner, Christian Xie, Zhi-Ping Staehelin, Christian |
author_facet | Xiang, Qi-Wang Bai, Juan Cai, Jie Huang, Qin-Ying Wang, Yan Liang, Ying Zhong, Zhi Wagner, Christian Xie, Zhi-Ping Staehelin, Christian |
author_sort | Xiang, Qi-Wang |
collection | PubMed |
description | Effectors secreted by the type III protein secretion system (T3SS) of rhizobia are host-specific determinants of the nodule symbiosis. Here, we have characterized NopD, a putative type III effector of Bradyrhizobium sp. XS1150. NopD was found to possess a functional N-terminal secretion signal sequence that could replace that of the NopL effector secreted by Sinorhizobium sp. NGR234. Recombinant NopD and the C-terminal domain of NopD alone can process small ubiquitin-related modifier (SUMO) proteins and cleave SUMO-conjugated proteins. Activity was abolished in a NopD variant with a cysteine-to-alanine substitution in the catalytic core (NopD-C(972)A). NopD recognizes specific plant SUMO proteins (AtSUMO1 and AtSUMO2 of Arabidopsis thaliana; GmSUMO of Glycine max; PvSUMO of Phaseolus vulgaris). Subcellular localization analysis with A. thaliana protoplasts showed that NopD accumulates in nuclear bodies. NopD, but not NopD-C(972)A, induces cell death when expressed in Nicotiana tabacum. Likewise, inoculation tests with constructed mutant strains of XS1150 indicated that nodulation of Tephrosia vogelii is negatively affected by the protease activity of NopD. In conclusion, our findings show that NopD is a symbiosis-related protein that can process specific SUMO proteins and desumoylate SUMO-conjugated proteins. |
format | Online Article Text |
id | pubmed-7098955 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-70989552020-04-07 NopD of Bradyrhizobium sp. XS1150 Possesses SUMO Protease Activity Xiang, Qi-Wang Bai, Juan Cai, Jie Huang, Qin-Ying Wang, Yan Liang, Ying Zhong, Zhi Wagner, Christian Xie, Zhi-Ping Staehelin, Christian Front Microbiol Microbiology Effectors secreted by the type III protein secretion system (T3SS) of rhizobia are host-specific determinants of the nodule symbiosis. Here, we have characterized NopD, a putative type III effector of Bradyrhizobium sp. XS1150. NopD was found to possess a functional N-terminal secretion signal sequence that could replace that of the NopL effector secreted by Sinorhizobium sp. NGR234. Recombinant NopD and the C-terminal domain of NopD alone can process small ubiquitin-related modifier (SUMO) proteins and cleave SUMO-conjugated proteins. Activity was abolished in a NopD variant with a cysteine-to-alanine substitution in the catalytic core (NopD-C(972)A). NopD recognizes specific plant SUMO proteins (AtSUMO1 and AtSUMO2 of Arabidopsis thaliana; GmSUMO of Glycine max; PvSUMO of Phaseolus vulgaris). Subcellular localization analysis with A. thaliana protoplasts showed that NopD accumulates in nuclear bodies. NopD, but not NopD-C(972)A, induces cell death when expressed in Nicotiana tabacum. Likewise, inoculation tests with constructed mutant strains of XS1150 indicated that nodulation of Tephrosia vogelii is negatively affected by the protease activity of NopD. In conclusion, our findings show that NopD is a symbiosis-related protein that can process specific SUMO proteins and desumoylate SUMO-conjugated proteins. Frontiers Media S.A. 2020-03-20 /pmc/articles/PMC7098955/ /pubmed/32265858 http://dx.doi.org/10.3389/fmicb.2020.00386 Text en Copyright © 2020 Xiang, Bai, Cai, Huang, Wang, Liang, Zhong, Wagner, Xie and Staehelin. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Xiang, Qi-Wang Bai, Juan Cai, Jie Huang, Qin-Ying Wang, Yan Liang, Ying Zhong, Zhi Wagner, Christian Xie, Zhi-Ping Staehelin, Christian NopD of Bradyrhizobium sp. XS1150 Possesses SUMO Protease Activity |
title | NopD of Bradyrhizobium sp. XS1150 Possesses SUMO Protease Activity |
title_full | NopD of Bradyrhizobium sp. XS1150 Possesses SUMO Protease Activity |
title_fullStr | NopD of Bradyrhizobium sp. XS1150 Possesses SUMO Protease Activity |
title_full_unstemmed | NopD of Bradyrhizobium sp. XS1150 Possesses SUMO Protease Activity |
title_short | NopD of Bradyrhizobium sp. XS1150 Possesses SUMO Protease Activity |
title_sort | nopd of bradyrhizobium sp. xs1150 possesses sumo protease activity |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7098955/ https://www.ncbi.nlm.nih.gov/pubmed/32265858 http://dx.doi.org/10.3389/fmicb.2020.00386 |
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