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Kelly, John [1], Takahashi, Gemma [2], Butts, Carter [3], Martin, Rachel [4].

Aspartic proteases from the Cape sundew, Drosera capensis: From genomic source code to functional diversity.

Aspartic proteases are endopeptidases that function best in acidic environments. In plants, they are used in a variety of contexts including protein processing, resistance to pathogens, drought response, and programmed cell death during senescence. In addition to these basic functions, carnivorous plants require a variety of proteases with different substrate affinities and cleavage sites to effectively digest the proteins from their prey. Aspartic proteases from carnivorous plants are attractive targets for characterization because they are likely to have different substrate preferences and activity profiles than the mammalian proteases typically used in biotechnology applications. These proteases are active at mildly acidic pH (5.5), and are therefore potentially useful as reagents in bottom-up proteomics applications.Here we explore the predicted structures and substrate specificities of seven aspartic proteases from the Cape sundew, Drosera capensis. The sequences were obtained from genomic DNA and investigated using bioinformatics techniques and molecular modeling.
We used protein structure prediction software followed by explicit-solvent molecular dynamics simulations to predict the three-dimensional structures of the putative aspartic proteases from D. capensis and from other plants for comparison. Many of the predicted proteins are homologous to known plant proteases, and contain both familiar and novel sequence and structural features. For example, several of the proteases have an unusual C-terminal domain that is not yet fully characterized. Further, many of the proteases contain a 100-amino acid sequence known as the plant-specific insert (PSI). This subsequence is cleaved after secretion, and acts as an antimicrobial peptide. Comparative analysis of PSIs from D. capensis aspartic proteases and those of other plants, such as the better-characterized potato and cardoon, will be discussed. Finally, experimental results from recombinantly expressed proteins will be presented.

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1 - UC Irvine, Chemistry, 1212 Natural Sciences 1, Irvine, CA, 92697-2025, United States
2 - UC Irvine, Molecular Biology & Biochemistry, 1403 Natural Sciences 1, Irvine, CA, 92697, USA
3 - UC Irvine, Statistics and Electrical Engineering & Computer Science, 3304 Calit2 Building, Irvine, CA, 92697
4 - University Of California, Irvine, Chemistry, 1102 Natural Sciences 2, Irvine, CA, 92697, United States

carnivorous plant
Drosera capensis
antimicrobial peptide
enzyme discovery.

Presentation Type: Oral Paper
Session: PHYT2, Phyochemistry II
Location: /
Date: Tuesday, July 20th, 2021
Time: 1:30 PM(EDT)
Number: PHYT2005
Abstract ID:535
Candidate for Awards:None

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