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GmDNJ1, a type‐I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean

Global warming poses severe threats to agricultural production, including soybean. One of the major mechanisms for organisms to combat heat stress is through heat shock proteins (HSPs) that stabilize protein structures at above‐optimum temperatures, by assisting in the folding of nascent, misfolded,...

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Autores principales: Li, Kwan‐Pok, Wong, Cheuk‐Hon, Cheng, Chun‐Chiu, Cheng, Sau‐Shan, Li, Man‐Wah, Mansveld, Sandra, Bergsma, Alex, Huang, Tengfang, van Eijk, Michiel J. T., Lam, Hon‐Ming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7833466/
https://www.ncbi.nlm.nih.gov/pubmed/33532690
http://dx.doi.org/10.1002/pld3.298
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author Li, Kwan‐Pok
Wong, Cheuk‐Hon
Cheng, Chun‐Chiu
Cheng, Sau‐Shan
Li, Man‐Wah
Mansveld, Sandra
Bergsma, Alex
Huang, Tengfang
van Eijk, Michiel J. T.
Lam, Hon‐Ming
author_facet Li, Kwan‐Pok
Wong, Cheuk‐Hon
Cheng, Chun‐Chiu
Cheng, Sau‐Shan
Li, Man‐Wah
Mansveld, Sandra
Bergsma, Alex
Huang, Tengfang
van Eijk, Michiel J. T.
Lam, Hon‐Ming
author_sort Li, Kwan‐Pok
collection PubMed
description Global warming poses severe threats to agricultural production, including soybean. One of the major mechanisms for organisms to combat heat stress is through heat shock proteins (HSPs) that stabilize protein structures at above‐optimum temperatures, by assisting in the folding of nascent, misfolded, or unfolded proteins. The HSP40 subgroups, or the J‐domain proteins, functions as co‐chaperones. They capture proteins that require folding or refolding and pass them on to HSP70 for processing. In this study, we have identified a type‐I HSP40 gene in soybean, GmDNJ1, with high basal expression under normal growth conditions and also highly inducible under abiotic stresses, especially heat. Gmdnj1‐knockout mutants had diminished growth in normal conditions, and when under heat stress, exhibited more severe browning, reduced chlorophyll contents, higher reactive oxygen species (ROS) contents, and higher induction of heat stress‐responsive transcription factors and ROS‐scavenging enzyme‐encoding genes. Under both normal and heat‐stress conditions, the mutant lines accumulated more aggregated proteins involved in protein catabolism, sugar metabolism, and membrane transportation, in both roots and leaves. In summary, GmDNJ1 plays crucial roles in the overall plant growth and heat tolerance in soybean, probably through the surveillance of misfolded proteins for refolding to maintain the full capacity of cellular functions.
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spelling pubmed-78334662021-02-01 GmDNJ1, a type‐I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean Li, Kwan‐Pok Wong, Cheuk‐Hon Cheng, Chun‐Chiu Cheng, Sau‐Shan Li, Man‐Wah Mansveld, Sandra Bergsma, Alex Huang, Tengfang van Eijk, Michiel J. T. Lam, Hon‐Ming Plant Direct Original Research Global warming poses severe threats to agricultural production, including soybean. One of the major mechanisms for organisms to combat heat stress is through heat shock proteins (HSPs) that stabilize protein structures at above‐optimum temperatures, by assisting in the folding of nascent, misfolded, or unfolded proteins. The HSP40 subgroups, or the J‐domain proteins, functions as co‐chaperones. They capture proteins that require folding or refolding and pass them on to HSP70 for processing. In this study, we have identified a type‐I HSP40 gene in soybean, GmDNJ1, with high basal expression under normal growth conditions and also highly inducible under abiotic stresses, especially heat. Gmdnj1‐knockout mutants had diminished growth in normal conditions, and when under heat stress, exhibited more severe browning, reduced chlorophyll contents, higher reactive oxygen species (ROS) contents, and higher induction of heat stress‐responsive transcription factors and ROS‐scavenging enzyme‐encoding genes. Under both normal and heat‐stress conditions, the mutant lines accumulated more aggregated proteins involved in protein catabolism, sugar metabolism, and membrane transportation, in both roots and leaves. In summary, GmDNJ1 plays crucial roles in the overall plant growth and heat tolerance in soybean, probably through the surveillance of misfolded proteins for refolding to maintain the full capacity of cellular functions. John Wiley and Sons Inc. 2021-01-25 /pmc/articles/PMC7833466/ /pubmed/33532690 http://dx.doi.org/10.1002/pld3.298 Text en © 2021 The Authors. Plant Direct published by American Society of Plant Biologists, Society for Experimental Biology and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
spellingShingle Original Research
Li, Kwan‐Pok
Wong, Cheuk‐Hon
Cheng, Chun‐Chiu
Cheng, Sau‐Shan
Li, Man‐Wah
Mansveld, Sandra
Bergsma, Alex
Huang, Tengfang
van Eijk, Michiel J. T.
Lam, Hon‐Ming
GmDNJ1, a type‐I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean
title GmDNJ1, a type‐I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean
title_full GmDNJ1, a type‐I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean
title_fullStr GmDNJ1, a type‐I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean
title_full_unstemmed GmDNJ1, a type‐I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean
title_short GmDNJ1, a type‐I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean
title_sort gmdnj1, a type‐i heat shock protein 40 (hsp40), is responsible for both growth and heat tolerance in soybean
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7833466/
https://www.ncbi.nlm.nih.gov/pubmed/33532690
http://dx.doi.org/10.1002/pld3.298
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