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Rice ubiquitin‐conjugating enzyme OsUbc13 negatively regulates immunity against pathogens by enhancing the activity of OsSnRK1a

Ubc13 is required for Lys63‐linked polyubiquitination and innate immune responses in mammals, but its functions in plant immunity still remain largely unknown. Here, we used molecular biological, pathological, biochemical, and genetic approaches to evaluate the roles of rice OsUbc13 in response to p...

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Autores principales: Liu, Jianping, Nie, Bo, Yu, Boling, Xu, Feiyun, Zhang, Qian, Wang, Ya, Xu, Weifeng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10363768/
https://www.ncbi.nlm.nih.gov/pubmed/37102249
http://dx.doi.org/10.1111/pbi.14059
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author Liu, Jianping
Nie, Bo
Yu, Boling
Xu, Feiyun
Zhang, Qian
Wang, Ya
Xu, Weifeng
author_facet Liu, Jianping
Nie, Bo
Yu, Boling
Xu, Feiyun
Zhang, Qian
Wang, Ya
Xu, Weifeng
author_sort Liu, Jianping
collection PubMed
description Ubc13 is required for Lys63‐linked polyubiquitination and innate immune responses in mammals, but its functions in plant immunity still remain largely unknown. Here, we used molecular biological, pathological, biochemical, and genetic approaches to evaluate the roles of rice OsUbc13 in response to pathogens. The OsUbc13‐RNA interference (RNAi) lines with lesion mimic phenotypes displayed a significant increase in the accumulation of flg22‐ and chitin‐induced reactive oxygen species, and in defence‐related genes expression or hormones as well as resistance to Magnaporthe oryzae and Xanthomonas oryzae pv oryzae. Strikingly, OsUbc13 directly interacts with OsSnRK1a, which is the α catalytic subunit of SnRK1 (sucrose non‐fermenting‐1‐related protein kinase‐1) and acts as a positive regulator of broad‐spectrum disease resistance in rice. In the OsUbc13‐RNAi plants, although the protein level of OsSnRK1a did not change, its activity and ABA sensitivity were obviously enhanced, and the K63‐linked polyubiquitination was weaker than that of wild‐type Dongjin (DJ). Overexpression of the deubiquitinase‐encoding gene OsOTUB1.1 produced similar effects with inhibition of OsUbc13 in affecting immunity responses, M. oryzae resistance, OsSnRK1a ubiquitination, and OsSnRK1a activity. Furthermore, re‐interfering with OsSnRK1a in one OsUbc13‐RNAi line (Ri‐3) partially restored its M. oryzae resistance to a level between those of Ri‐3 and DJ. Our data demonstrate OsUbc13 negatively regulates immunity against pathogens by enhancing the activity of OsSnRK1a.
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spelling pubmed-103637682023-07-25 Rice ubiquitin‐conjugating enzyme OsUbc13 negatively regulates immunity against pathogens by enhancing the activity of OsSnRK1a Liu, Jianping Nie, Bo Yu, Boling Xu, Feiyun Zhang, Qian Wang, Ya Xu, Weifeng Plant Biotechnol J Research Articles Ubc13 is required for Lys63‐linked polyubiquitination and innate immune responses in mammals, but its functions in plant immunity still remain largely unknown. Here, we used molecular biological, pathological, biochemical, and genetic approaches to evaluate the roles of rice OsUbc13 in response to pathogens. The OsUbc13‐RNA interference (RNAi) lines with lesion mimic phenotypes displayed a significant increase in the accumulation of flg22‐ and chitin‐induced reactive oxygen species, and in defence‐related genes expression or hormones as well as resistance to Magnaporthe oryzae and Xanthomonas oryzae pv oryzae. Strikingly, OsUbc13 directly interacts with OsSnRK1a, which is the α catalytic subunit of SnRK1 (sucrose non‐fermenting‐1‐related protein kinase‐1) and acts as a positive regulator of broad‐spectrum disease resistance in rice. In the OsUbc13‐RNAi plants, although the protein level of OsSnRK1a did not change, its activity and ABA sensitivity were obviously enhanced, and the K63‐linked polyubiquitination was weaker than that of wild‐type Dongjin (DJ). Overexpression of the deubiquitinase‐encoding gene OsOTUB1.1 produced similar effects with inhibition of OsUbc13 in affecting immunity responses, M. oryzae resistance, OsSnRK1a ubiquitination, and OsSnRK1a activity. Furthermore, re‐interfering with OsSnRK1a in one OsUbc13‐RNAi line (Ri‐3) partially restored its M. oryzae resistance to a level between those of Ri‐3 and DJ. Our data demonstrate OsUbc13 negatively regulates immunity against pathogens by enhancing the activity of OsSnRK1a. John Wiley and Sons Inc. 2023-04-27 2023-08 /pmc/articles/PMC10363768/ /pubmed/37102249 http://dx.doi.org/10.1111/pbi.14059 Text en © 2023 The Authors. Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Liu, Jianping
Nie, Bo
Yu, Boling
Xu, Feiyun
Zhang, Qian
Wang, Ya
Xu, Weifeng
Rice ubiquitin‐conjugating enzyme OsUbc13 negatively regulates immunity against pathogens by enhancing the activity of OsSnRK1a
title Rice ubiquitin‐conjugating enzyme OsUbc13 negatively regulates immunity against pathogens by enhancing the activity of OsSnRK1a
title_full Rice ubiquitin‐conjugating enzyme OsUbc13 negatively regulates immunity against pathogens by enhancing the activity of OsSnRK1a
title_fullStr Rice ubiquitin‐conjugating enzyme OsUbc13 negatively regulates immunity against pathogens by enhancing the activity of OsSnRK1a
title_full_unstemmed Rice ubiquitin‐conjugating enzyme OsUbc13 negatively regulates immunity against pathogens by enhancing the activity of OsSnRK1a
title_short Rice ubiquitin‐conjugating enzyme OsUbc13 negatively regulates immunity against pathogens by enhancing the activity of OsSnRK1a
title_sort rice ubiquitin‐conjugating enzyme osubc13 negatively regulates immunity against pathogens by enhancing the activity of ossnrk1a
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10363768/
https://www.ncbi.nlm.nih.gov/pubmed/37102249
http://dx.doi.org/10.1111/pbi.14059
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