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

Contour-Ansel, Dominique; Torres-Franklin, Maria Lucia; Zuily-Fodil, Yasmine; Carvalho, Maria Helena Cruz de

doi:10.1016/j.jplph.2010.06.018

Cited by 28 publications

(12 citation statements)

References 49 publications

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“…Pepsin‐like aspartic proteases are subdivided into subfamilies A1 (typical pepsin‐like), A2 (typical, but lacking the plant‐specific insert), B (nucellins) and C (atypical) (Faro and Gal, ). We detected transcripts and identified peptides for 10 A1 pepsin‐like proteases and they cluster with two enzymes implicated in stress responses, barley phythepsin and bean AP1 (Contour‐Ansel et al ., ; Hückelhoven et al ., ). Group A2 seems absent in the N. benthamiana predicted proteome.…”

Section: Resultsmentioning

confidence: 98%

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

Grosse‐Holz

Kelly

Blaskowski

et al. 2017

Plant Biotechnology Journal

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SummaryInfiltration of disarmed Agrobacterium tumefaciens into leaves of Nicotiana benthamiana (agroinfiltration) facilitates quick and safe production of antibodies, vaccines, enzymes and metabolites for industrial use (molecular farming). However, yield and purity of proteins produced by agroinfiltration are hampered by unintended proteolysis, restricting industrial viability of the agroinfiltration platform. Proteolysis may be linked to an immune response to agroinfiltration, but understanding of the response to agroinfiltration is limited. To identify the proteases, we studied the transcriptome, extracellular proteome and active secretome of agroinfiltrated leaves over a time course, with and without the P19 silencing inhibitor. Remarkably, the P19 expression had little effect on the leaf transcriptome and no effect on the extracellular proteome. 25% of the detected transcripts changed in abundance upon agroinfiltration, associated with a gradual up‐regulation of immunity at the expense of photosynthesis. By contrast, 70% of the extracellular proteins increased in abundance, in many cases associated with increased efficiency of extracellular delivery. We detect a dynamic reprogramming of the proteolytic machinery upon agroinfiltration by detecting transcripts encoding for 975 different proteases and protease homologs. The extracellular proteome contains peptides derived from 196 proteases and protease homologs, and activity‐based proteomics displayed 17 active extracellular Ser and Cys proteases in agroinfiltrated leaves. We discuss unique features of the N. benthamiana protease repertoire and highlight abundant extracellular proteases in agroinfiltrated leaves, being targets for reverse genetics. This data set increases our understanding of the plant response to agroinfiltration and indicates ways to improve a key expression platform for both plant science and molecular farming.

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Section: Resultsmentioning

confidence: 98%

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

Grosse‐Holz

Kelly

Blaskowski

et al. 2017

Plant Biotechnology Journal

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“…In plants, they are involved in many biological processes, including senescence, stress responses, programmed cell death, and reproduction (Chen et al, 2009;Guo et al, 2013). According to Contour-Ansel et al (2010), water stress in bean led to the gene expression regulation of an AP gene (PvAP1) both at the transcriptional and post-transcriptional levels, which is paramount in the conservation of cellular homeostasis and recovery. In other experiment examining drought in Arabidopsis, Yao et al (2012) identified an AP gene (ASPG1) that may function in drought avoidance through ABA signaling in guard cells.…”

Section: Discussionmentioning

confidence: 99%

Differential gene expression in drought-tolerant sugarcane roots

et al. 2015

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ABSTRACT. Drought is one of the most frequent abiotic stresses limiting the productivity and geographical distribution of sugarcane culture. The use of drought-tolerant genotypes is one approach for overcoming the effects of water stress. We conducted a comparative study to identify gene expression profiles under water stress in tolerant sugarcane roots. Two different cultivars, 1 drought tolerant (RB867515) and 1 drought susceptible (SP86-155), were evaluated at 4 sampling time points (1, 3, 5, and 10 days) using the cDNA-amplified fragment length polymorphism technique. A total of 173 fragments were found to be differentially expressed in response to water stress in the tolerant cultivar. Seventy of these were cloned, sequenced, and categorized. Similarity analysis using Candidate genes to drought tolerance in sugarcane BLAST revealed that 64% of the fragments differentially expressed code proteins classified as no hits (23%), hypothetical (21%), or involved in stress response (20%), with others were involved in communication pathways and signal transduction, bioenergetics, secondary metabolism, and growth and development. Four genes were analyzed and validated using real-time quantitative polymerase chain reaction to determine their expression and showed consistency with the cDNA-amplified fragment length polymorphism analyses. Our results contribute insight into the molecular responses to water stress in sugarcane and possibility to the development of cultivars with improved tolerance to drought.

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“…For the majority of the plant proteases, the proteolytic activity and substrate specificity are yet unknown (van der Hoorn, 2008), but presumably several of these will have trypsinelike specificity. Some of the plant proteases are also expressed in direct response to water stress (Contour-Ansel et al, 2010). Even so, the role of proteolytic cleavage in modulating membrane binding of dehydrins in vivo remains at this stage speculative and needs further experimental evaluation.…”

Section: Luvs Do Not Protect Lti30 Against Protease Degradation But mentioning

confidence: 99%

Tunable Membrane Binding of the Intrinsically Disordered Dehydrin Lti30, a Cold-Induced Plant Stress Protein

et al. 2011

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Dehydrins are intrinsically disordered plant proteins whose expression is upregulated under conditions of desiccation and cold stress. Their molecular function in ensuring plant survival is not yet known, but several studies suggest their involvement in membrane stabilization. The dehydrins are characterized by a broad repertoire of conserved and repetitive sequences, out of which the archetypical K-segment has been implicated in membrane binding. To elucidate the molecular mechanism of these K-segments, we examined the interaction between lipid membranes and a dehydrin with a basic functional sequence composition: Lti30, comprising only K-segments. Our results show that Lti30 interacts electrostatically with vesicles of both zwitterionic (phosphatidyl choline) and negatively charged phospholipids (phosphatidyl glycerol, phosphatidyl serine, and phosphatidic acid) with a stronger binding to membranes with high negative surface potential. The membrane interaction lowers the temperature of the main lipid phase transition, consistent with Lti30's proposed role in cold tolerance. Moreover, the membrane binding promotes the assembly of lipid vesicles into large and easily distinguishable aggregates. Using these aggregates as binding markers, we identify three factors that regulate the lipid interaction of Lti30 in vitro: (1) a pH dependent His on/off switch, (2) phosphorylation by protein kinase C, and (3) reversal of membrane binding by proteolytic digest.

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

Cited by 28 publications

References 49 publications

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

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

Differential gene expression in drought-tolerant sugarcane roots

Tunable Membrane Binding of the Intrinsically Disordered Dehydrin Lti30, a Cold-Induced Plant Stress Protein

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