The thiol-disulfide exchange activity of AtPDI1 is involved in the response to abiotic stresses
Abstract Background Arabidopsis protein disulfide isomerase 1 (AtPDI1) has been demonstrated to have disulfide isomerase activity and to be involved in the stress response. However, whether the anti-stress function is directly related to the activities of thiol-disulfide exchange remains to be eluci...
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Autores principales: | , , , , , , |
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Formato: | article |
Lenguaje: | EN |
Publicado: |
BMC
2021
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Materias: | |
Acceso en línea: | https://doaj.org/article/54bc969797a449ad9b2a83234ec606c6 |
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Sumario: | Abstract Background Arabidopsis protein disulfide isomerase 1 (AtPDI1) has been demonstrated to have disulfide isomerase activity and to be involved in the stress response. However, whether the anti-stress function is directly related to the activities of thiol-disulfide exchange remains to be elucidated. Results In the present study, encoding sequences of AtPDI1 of wild-type (WT) and double-cysteine-mutants were transformed into an AtPDI1 knockdown Arabidopsis line (pdi), and homozygous transgenic plants named pdi-AtPDI1, pdi-AtPDI1m1 and pdi-AtPDI1m2 were obtained. Compared with the WT and pdi-AtPDI1, the respective germination ratios of pdi-AtPDI1m1 and pdi-AtPDI1m2 were significantly lower under abiotic stresses and exogenous ABA treatment, whereas the highest germination rate was obtained with AtPDI1 overexpression in the WT (WT- AtPDI1). The root length among different lines was consistent with the germination rate; a higher germination rate was observed with a longer root length. When seedlings were treated with salt, drought, cold and high temperature stresses, pdi-AtPDI1m1, pdi-AtPDI1m2 and pdi displayed lower survival rates than WT and AtPDI1 overexpression plants. The transcriptional levels of ABA-responsive genes and genes encoding ROS-quenching enzymes were lower in pdi-AtPDI1m1 and pdi-AtPDI1m2 than in pdi-AtPDI1. Conclusion Taken together, these results clearly suggest that the anti-stress function of AtPDI1 is directly related to the activity of disulfide isomerase. |
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