IBIOS-EPM, UMR CNRS 7618 BIOEMCO, Université Paris Est-Paris 12, 61 Avenue du Général de Gaulle, F-94010 Créteil Cedex, France.
J Plant Physiol. 2010 Dec 15;167(18):1606-12. doi: 10.1016/j.jplph.2010.06.018. Epub 2010 Aug 11.
A cDNA encoding a putative aspartic acid protease precursor (PvAP1) was cloned from the leaves of common bean (Phaseolus vulgaris). Sequence analysis showed that PvAP1 presents all the characteristic features of phytepsins, the typical plant APs. PvAP1 gene expression was tightly regulated by water stress, being significantly up-regulated under mild water stress (Ψ(w)=-1.0 MPa) for the drought-susceptible cultivar (Carioca) and moderate water stress (Ψ(w)=-1.5 MPa) for the more drought-tolerant cultivar (IPA). Protein gel blotting analysis under water stress revealed the presence of two main bands of calculated MW of 46 and 38 kDa, suggesting proteolytic processing of the enzyme precursor form under drought in both cultivars. Taken together, our results suggest that water stress regulates PvAP1 activity both at the transcriptional and post-transcriptional levels, and that the response occurs earlier and is stronger in the drought-susceptible cultivar.
从普通菜豆（Phaseolus vulgaris）叶片中克隆出一个编码假定天冬氨酸蛋白酶前体（PvAP1）的 cDNA。序列分析表明，PvAP1 具有植物天冬氨酸蛋白酶的所有特征。PvAP1 基因表达受水分胁迫的严格调控，在干旱敏感品种（Carioca）轻度水分胁迫（Ψ（w）=-1.0 MPa）和更耐旱品种（IPA）中度水分胁迫（Ψ（w）=-1.5 MPa）下显著上调。水分胁迫下的蛋白质凝胶印迹分析显示存在两个主要的计算 MW 为 46 和 38 kDa 的条带，表明在两个品种中，干旱条件下酶前体形式发生了蛋白水解加工。综上所述，我们的结果表明，水分胁迫在转录和转录后水平上调节 PvAP1 的活性，并且在干旱敏感品种中，该反应发生得更早且更强。
