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Enhanced Accumulation of BnA7HSP70 Molecular Chaperone Binding Protein Improves Tolerance to Drought Stress in Transgenic Brassica napus
Li-Li WAN, Zhuan-Rong WANG, Qiang XIN, Fa-Ming DONG, Deng-Feng HONG, Guang-Sheng YANG
Acta Agronomica Sinica    2018, 44 (04): 483-492.   DOI: 10.3724/SP.J.1006.2018.00483
Abstract   (625 HTML11 PDF(pc) (5501KB)(716)  

The molecular chaperone binding protein gene participates in the constitutive function of plant growth and protects plant cells against stresses. In this study, we found that BnA7HSP70 overexpressed transgenic lines did not wilt and showed only a small decrease in water potential. However, the wild type lines showed a large decrease in leaf water potential. The transgenic plants had higher relative water content, better osmotic adjustment and less lipid membrane peroxidation. In addition, the leaves from the elevated levels of BnA7HSP70 in transgenic lines conferred tolerance to the glycosylation inhibitor tunicamycin during germination. BnA7HSP70 overexpression-mediated attenuation of stress-induced cell death was confirmed by the decreased percentage of dead cell and the reduced induction of the senescence-associated marker gene BnCNX1. These phenotypes were accompanied by a delay in the induction of the cell death marker genes BnNRP, which are involved in transducing a cell death signal generated by ER stress and osmotic stress through the NRP (N-rich protein)-mediated signaling pathway. Enhanced expression of BnA7HSP70 delayed unfold protein response and NRP pathway mediated chlorosis and the appearance of senescence-associated markers BnLSC222 and BnLSC54 in Brassica napus. These results suggest that overexpression of BnA7HSP70 in Brassica napus alleviate ER stress and osmotic stress-integrating cell death response confronted with water stress.


Fig. 9 Model for BnA7HSP70 expression on the mobilization of bZIP28 and upregulation of UPR genes
(A) In response to the stress, BnA7HSP70 is competed away by the accumulation of misfolded proteins and bZIP28 is proteolytically activated by Golgi-localized S1P or S2P to release bZIP28n, which relocates to the nucleus where it upregulates stress genes including BnBiP3 and BnCNX1; (B) When BnA7HSP70 is overexpressed, accumulated BnA7HSP70 is enough for association with bZIP28 and misfolded proteins. As a result, bZIP28 is detained in the ER even under stress conditions.
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图9   BnA7HSP70调控bZIP 28基因介导的未折叠蛋白途径的模式
(A)在逆境胁迫下, BnA7HSP70蛋白与未折叠蛋白结合后从bZIP 28中释放下来, 定位于高尔基体的S1P和S2P将bZIP 28蛋白水解后释放得到bZIP 28n, 转录因子bZIP 28n定位到细胞核中上调BnBiP3BnCNX1基因的表达; (B)当BnA7HSP70超表达后, 得到足够的BnA7HSP70蛋白质与bZIP28和胁迫下产生的未折叠蛋白结合, 使得bZIP28保留在内质网上, 从而不会上调细胞核中基因的表达。
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