An aspartic acid protease from common bean is expressed 'on call' during water stress and early recovery

被引:29
作者
Contour-Ansel, Dominique [1 ]
Torres-Franklin, Maria Lucia [1 ]
Zuily-Fodil, Yasmine [1 ]
de Carvalho, Maria Helena Cruz [1 ]
机构
[1] Univ Paris 12, BIOEMCO, CNRS, IBIOS EPM,UMR 7618, F-94010 Creteil, France
关键词
Phaseolus vulgaris; Proteolysis; Drought tolerance; Phytepsins; Gene expression; PHASEOLUS-VULGARIS L; MOLECULAR-CLONING; ENZYMATIC-ACTIVITY; GENE STRUCTURE; SPRING WHEAT; PROTEINASE; DROUGHT; LEAVES; CARDOSIN; COWPEA;
D O I
10.1016/j.jplph.2010.06.018
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
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 (Psi(w) = -1.0 MPa) for the drought-susceptible cultivar (Carioca) and moderate water stress (Psi(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. (C) 2010 Elsevier GmbH. All rights reserved.
引用
收藏
页码:1606 / 1612
页数:7
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