PUB63, a novel early heat responsive ubiquitin E3 ligase from rice implicates heat stress tolerance
Heat stress has emerged as a major environmental challenge triggering reduced crop yields, compromised growth, and negatively affecting the development of crops. The cellular response to heat stress involves transcriptional and translational reprogramming and regulation of protein homeostasis which...
Main Authors: | , , , |
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Format: | Article |
Language: | English |
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Elsevier
2023-12-01
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Series: | Plant Stress |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2667064X23001586 |
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author | Harmeet Kaur Prafull Salvi Akansha Chaurasia Tapan K. Mondal |
author_facet | Harmeet Kaur Prafull Salvi Akansha Chaurasia Tapan K. Mondal |
author_sort | Harmeet Kaur |
collection | DOAJ |
description | Heat stress has emerged as a major environmental challenge triggering reduced crop yields, compromised growth, and negatively affecting the development of crops. The cellular response to heat stress involves transcriptional and translational reprogramming and regulation of protein homeostasis which is crucial for the heat stress response and leads to the differential expression of many genes associated with protein turnover mechanisms. Plant U-box (PUB) proteins are a class of the Ubiquitin-E3 ligase involved in the Ubiquitin-proteasome pathway. In the present study, we investigated the role of a PUB protein from rice, OsPUB63, involved in heat stress responses in rice. We also identified all PUB coding genes from O. sativa indica and compared with O. sativa japonica. A quantitative real time PCR demonstrated, OsPUB63 as an early heat inducible gene in rice and the subcellular localization study confirmed its presence in the nucleus and cytosol. OsPUB63 was demonstrated as a TPR repeat containing protein with molecular weight of 39.3 KDa. Using a combination of genetic, biochemical, and physiological assays, our work establishes OsPUB63 as crucial in regulating the heat stress response in rice. Specifically, we show that OsPUB63 enhances the heat stress tolerance in transgenic Arabidopsis by promoting the accumulation of proline and reduced MDA content. Our work has identified PUB63 as the first PUB gene family E3 ligase from rice which is implicated in heat stress response and provide a crucial target for improving crop yields under high-temperature conditions in rice. |
first_indexed | 2024-03-09T07:33:23Z |
format | Article |
id | doaj.art-941df9d465cd4735a1cee9494dd30917 |
institution | Directory Open Access Journal |
issn | 2667-064X |
language | English |
last_indexed | 2024-03-09T07:33:23Z |
publishDate | 2023-12-01 |
publisher | Elsevier |
record_format | Article |
series | Plant Stress |
spelling | doaj.art-941df9d465cd4735a1cee9494dd309172023-12-03T05:43:41ZengElsevierPlant Stress2667-064X2023-12-0110100291PUB63, a novel early heat responsive ubiquitin E3 ligase from rice implicates heat stress toleranceHarmeet Kaur0Prafull Salvi1Akansha Chaurasia2Tapan K. Mondal3ICAR-National Institute for Plant Biotechnology, New Delhi, India; Corresponding author.National Agri-Food Biotechnology Institute, Mohali, IndiaICAR-National Institute for Plant Biotechnology, New Delhi, IndiaICAR-National Institute for Plant Biotechnology, New Delhi, IndiaHeat stress has emerged as a major environmental challenge triggering reduced crop yields, compromised growth, and negatively affecting the development of crops. The cellular response to heat stress involves transcriptional and translational reprogramming and regulation of protein homeostasis which is crucial for the heat stress response and leads to the differential expression of many genes associated with protein turnover mechanisms. Plant U-box (PUB) proteins are a class of the Ubiquitin-E3 ligase involved in the Ubiquitin-proteasome pathway. In the present study, we investigated the role of a PUB protein from rice, OsPUB63, involved in heat stress responses in rice. We also identified all PUB coding genes from O. sativa indica and compared with O. sativa japonica. A quantitative real time PCR demonstrated, OsPUB63 as an early heat inducible gene in rice and the subcellular localization study confirmed its presence in the nucleus and cytosol. OsPUB63 was demonstrated as a TPR repeat containing protein with molecular weight of 39.3 KDa. Using a combination of genetic, biochemical, and physiological assays, our work establishes OsPUB63 as crucial in regulating the heat stress response in rice. Specifically, we show that OsPUB63 enhances the heat stress tolerance in transgenic Arabidopsis by promoting the accumulation of proline and reduced MDA content. Our work has identified PUB63 as the first PUB gene family E3 ligase from rice which is implicated in heat stress response and provide a crucial target for improving crop yields under high-temperature conditions in rice.http://www.sciencedirect.com/science/article/pii/S2667064X23001586Abiotic stressArabidopsisPUBReal-time PCRSubcellular localizationTransgenics |
spellingShingle | Harmeet Kaur Prafull Salvi Akansha Chaurasia Tapan K. Mondal PUB63, a novel early heat responsive ubiquitin E3 ligase from rice implicates heat stress tolerance Plant Stress Abiotic stress Arabidopsis PUB Real-time PCR Subcellular localization Transgenics |
title | PUB63, a novel early heat responsive ubiquitin E3 ligase from rice implicates heat stress tolerance |
title_full | PUB63, a novel early heat responsive ubiquitin E3 ligase from rice implicates heat stress tolerance |
title_fullStr | PUB63, a novel early heat responsive ubiquitin E3 ligase from rice implicates heat stress tolerance |
title_full_unstemmed | PUB63, a novel early heat responsive ubiquitin E3 ligase from rice implicates heat stress tolerance |
title_short | PUB63, a novel early heat responsive ubiquitin E3 ligase from rice implicates heat stress tolerance |
title_sort | pub63 a novel early heat responsive ubiquitin e3 ligase from rice implicates heat stress tolerance |
topic | Abiotic stress Arabidopsis PUB Real-time PCR Subcellular localization Transgenics |
url | http://www.sciencedirect.com/science/article/pii/S2667064X23001586 |
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