Literature DB >> 20705361

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

Dominique Contour-Ansel1, Maria Lucia Torres-Franklin, Yasmine Zuily-Fodil, Maria Helena Cruz de Carvalho.   

Abstract

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.
Copyright © 2010 Elsevier GmbH. All rights reserved.

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Year:  2010        PMID: 20705361     DOI: 10.1016/j.jplph.2010.06.018

Source DB:  PubMed          Journal:  J Plant Physiol        ISSN: 0176-1617            Impact factor:   3.549


  6 in total

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6.  The transcriptome, extracellular proteome and active secretome of agroinfiltrated Nicotiana benthamiana uncover a large, diverse protease repertoire.

Authors:  Friederike Grosse-Holz; Steven Kelly; Svenja Blaskowski; Farnusch Kaschani; Markus Kaiser; Renier A L van der Hoorn
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  6 in total

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