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<p>Extreme temperature stress caused by global climate change markedly reduces forage grass production. Enhancing thermotolerance in these plants can therefore boost yields and ensure agricultural sustainability. The Hsp70 family of molecular chaperones is vital for plant stress resilience. In this study, we characterized the <i>LcHsp70-1</i> gene in <i>Lotus corniculatus</i> to assess its role in temperature stress tolerance. Bioinformatics analysis showed that <i>LcHsp70-1</i> encodes a hydrophilic, stable 73.77&#xa0;kDa protein and possesses a promoter containing cold- and drought-responsive elements. The protein is predicted to interact with several members of the Hsp40, Hsp70, and Hsp90 subfamilies. Transgenic plants (TP) overexpressing <i>LcHsp70-1</i> exhibited better stress resistance than wild-type plants (WT) under both 42&#xa0;°C and 4&#xa0;°C stresses. In TP, relative electrical conductivity decreased by 52% and 26%, and malondialdehyde (MDA) content declined by 34% and 30%, respectively. Concurrently, the activities of key antioxidant enzymes increased: superoxide dismutase (SOD) by 37% and 24%, catalase (CAT) by 11% and 39%, and peroxidase (POD) by 52% and 48%. qRT-PCR analysis further showed that <i>LcHsp70-1</i> overexpression modulates stress-associated transcription factors. Under high-temperature stress (42&#xa0;°C), expression of <i>LcMIKC-MADS</i> and <i>LcbHLH</i> was downregulated. At low-temperature stress (4&#xa0;°C), <i>LcMIKC-MADS</i> and <i>LcSBP</i> were reduced. <i>LcG2-like</i> was upregulated under both conditions, implying a crucial role in stress resistance. Collectively, our findings demonstrate that <i>LcHsp70-1</i> enhances heat and cold tolerance in <i>Lotus corniculatus</i> through three pathways: (1) chaperone-mediated protein quality control, (2) enhancement of the antioxidant defense system, and (3) modulation of stress-responsive transcription factors.</p>

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Functional analysis of LcHsp70-1 in enhancing temperature stress tolerance in Lotus corniculatus

  • 期刊论文

  • 发表日期：

    2026年1月21日

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  • Yilong Li,
  • Jing Liu,
  • Zouxian Gong,
  • Ying Xu,
  • Jiahai Wu,
  • Li Song

摘要

Extreme temperature stress caused by global climate change markedly reduces forage grass production. Enhancing thermotolerance in these plants can therefore boost yields and ensure agricultural sustainability. The Hsp70 family of molecular chaperones is vital for plant stress resilience. In this study, we characterized the LcHsp70-1 gene in Lotus corniculatus to assess its role in temperature stress tolerance. Bioinformatics analysis showed that LcHsp70-1 encodes a hydrophilic, stable 73.77 kDa protein and possesses a promoter containing cold- and drought-responsive elements. The protein is predicted to interact with several members of the Hsp40, Hsp70, and Hsp90 subfamilies. Transgenic plants (TP) overexpressing LcHsp70-1 exhibited better stress resistance than wild-type plants (WT) under both 42 °C and 4 °C stresses. In TP, relative electrical conductivity decreased by 52% and 26%, and malondialdehyde (MDA) content declined by 34% and 30%, respectively. Concurrently, the activities of key antioxidant enzymes increased: superoxide dismutase (SOD) by 37% and 24%, catalase (CAT) by 11% and 39%, and peroxidase (POD) by 52% and 48%. qRT-PCR analysis further showed that LcHsp70-1 overexpression modulates stress-associated transcription factors. Under high-temperature stress (42 °C), expression of LcMIKC-MADS and LcbHLH was downregulated. At low-temperature stress (4 °C), LcMIKC-MADS and LcSBP were reduced. LcG2-like was upregulated under both conditions, implying a crucial role in stress resistance. Collectively, our findings demonstrate that LcHsp70-1 enhances heat and cold tolerance in Lotus corniculatus through three pathways: (1) chaperone-mediated protein quality control, (2) enhancement of the antioxidant defense system, and (3) modulation of stress-responsive transcription factors.