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
相关论文
共 47 条
[1]   Aspartic proteinases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco [J].
An, CI ;
Fukusaki, E ;
Kobayashi, A .
PLANTA, 2002, 214 (05) :661-667
[2]   Oryzasin as an aspartic proteinase occurring in rice seeds: Purification, characterization, and application to milk clotting [J].
Asakura, T ;
Watanabe, H ;
Abe, K ;
Arai, S .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1997, 45 (04) :1070-1075
[3]   The plant aspartic proteinase-specific polypeptide insert is not directly related to the activity of oryzasin 1 [J].
Asakura, T ;
Matsumoto, I ;
Funaki, J ;
Arai, S ;
Abe, K .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (16) :5115-5122
[4]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[5]   Activation, proteolytic processing, and peptide specificity of recombinant cardosin A [J].
Castanheira, P ;
Samyn, B ;
Sergeant, K ;
Clemente, JC ;
Dunn, BM ;
Pires, E ;
Van Beeumen, J ;
Faro, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (13) :13047-13054
[6]   Aspartic proteases gene family in rice: Gene structure and expression, predicted protein features and phylogenetic relation [J].
Chen, Jiongjiong ;
Ouyang, Yidan ;
Wang, Lei ;
Xie, Weibo ;
Zhang, Qifa .
GENE, 2009, 442 (1-2) :108-118
[7]   Glutathione reductase in leaves of cowpea: Cloning of two cDNAs, expression and enzymatic activity under progressive drought stress, desiccation and abscisic acid treatment [J].
Contour-Ansel, Dominique ;
Torres-Franklin, Maria Lucia ;
Cruz De Carvalho, Maria Helena ;
D'Arcy-Lameta, Agnes .
ANNALS OF BOTANY, 2006, 98 (06) :1279-1287
[8]   Isolation and characterization of an aspartic proteinase gene from cowpea (Vigna unguiculata L. Walp.) [J].
de Carvalho, MHC ;
Pham-Thi, AT ;
Gareil, M ;
d'Arcy-Lameta, A ;
Fodil, YZ .
JOURNAL OF PLANT PHYSIOLOGY, 2004, 161 (08) :971-976
[9]   Aspartic protease in leaves of common bean (Phaseolus vulgaris L.) and cowpea (Vigna unguiculata L. Walp):: enzymatic activity, gene expression and relation to drought susceptibility [J].
de Carvalho, MHC ;
d'Arcy-Lameta, A ;
Roy-Macauley, H ;
Gareil, M ;
El Maarouf, H ;
Pham-Thi, AT ;
Zuily-Fodil, Y .
FEBS LETTERS, 2001, 492 (03) :242-246
[10]  
Domingos A, 2000, EUR J BIOCHEM, V267, P6824, DOI 10.1046/j.1432-1327.2000.01780.x