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玉米( L.)抗旱性转化酶抑制剂的功能特征。

Functional Characterization of a Drought-Responsive Invertase Inhibitor from Maize ( L.).

机构信息

College of Horticulture, South China Agricultural University, Guangzhou 510642, China.

Centre for Organismal Studies Heidelberg, Department of Plant Molecular Physiology, University of Heidelberg, 69120 Heidelberg, Germany.

出版信息

Int J Mol Sci. 2019 Aug 21;20(17):4081. doi: 10.3390/ijms20174081.

Abstract

Invertases (INVs) play essential roles in plant growth in response to environmental cues. Previous work showed that plant invertases can be post-translationally regulated by small protein inhibitors (INVINHs). Here, this study characterizes a proteinaceous inhibitor of INVs in maize (Zm-INVINH4). A functional analysis of the recombinant Zm-INVINH4 protein revealed that it inhibited both cell wall and vacuolar invertase activities from maize leaves. A Zm-INVINH4::green fluorescent protein fusion experiment indicated that this protein localized in the apoplast. Transcript analysis showed that is specifically expressed in maize sink tissues, such as the base part of the leaves and young kernels. Moreover, drought stress perturbation significantly induced expression, which was accompanied with a decrease of cell wall invertase (CWI) activities and an increase of sucrose accumulation in both base parts of the leaves 2 to 7 days after pollinated kernels. In summary, the results support the hypothesis that INV-related sink growth in response to drought treatment is (partially) caused by a silencing of INV activity via drought-induced induction of Zm-INVINH4 protein.

摘要

转化酶(INV)在植物响应环境信号的生长中发挥重要作用。先前的工作表明,植物转化酶可以通过小蛋白抑制剂(INVINHs)进行翻译后调控。本研究在玉米中鉴定到一种INV 的蛋白抑制剂(Zm-INVINH4)。对重组Zm-INVINH4 蛋白的功能分析表明,它抑制了玉米叶片的细胞壁和液泡转化酶活性。Zm-INVINH4::绿色荧光蛋白融合实验表明,该蛋白定位于质外体。转录分析表明,在玉米的库组织中特异性表达,如叶片基部和幼嫩的穗部。此外,干旱胁迫处理显著诱导了 的表达,伴随着授粉后 2 至 7 天叶片基部细胞壁转化酶(CWI)活性的降低和蔗糖积累的增加。总之,这些结果支持了这样的假设,即响应干旱处理的与 INV 相关的库生长是(部分)通过干旱诱导Zm-INVINH4 蛋白的表达而导致 INV 活性沉默引起的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5dbe/6747265/cbd1d53d73a3/ijms-20-04081-g001.jpg

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