Abstract
A novel type of aspartic proteinase gene was isolated from the cDNA library of developing buckwheat seeds. This cDNA, FeAPL1, encoded an AP-like protein lacking the plant-specific insert (PSI) domain characteristic of typical plant aspartic proteinases. In addition the corresponding genomic fragment was isolated. It is demonstrated that this gene does not contain introns. Since bioinformatics analysis of the Arabidopsis genome showed that most potential AP genes are intronless and PSI-less, it appears that "atypical" is an inappropriate word for that class of AP. Isolation of this specific buckwheat gene among the small group of those isolated from other plant species provides a new perspective on the diversity of AP family members in plants. .
Highlights
Proteolytic enzymes are intricately involved in many aspects of plant physiology and development and are the subject of intensive research interest
We report the isolation from buckwheat of fulllength cDNA coding for a specific type of aspartic proteinases, one that could be relegated to the category of the much less explored plant APs characterized by the lack of a plant-specific insert (PSI) region
According to the MEROPS database, the majority of plant APs belong to the pepsin-like (A1) family
Summary
Proteolytic enzymes are intricately involved in many aspects of plant physiology and development and are the subject of intensive research interest. Plant APs have been detected or purified from monocotyledonous and dicotyledonous species as well as gymnosperms (Mutlu and G a l, 1999) as proteases which are most active at acidic pH, are inhibited by pepstatin A, and contain two aspartic acid residues indispensable for catalytic activity. They are typically distinguished from their non-plant homologs by the presence of a so-called plant-specific insert (PSI), which is removed during processing and is absent from most mature plant APs. there are exceptions to this well-known primary structural organization. Bioinformatics analysis of the Arabidopsis genome sequence revealed 59 AP-like proteins, which provides a new perspective on the diversity of AP family members in plants (Beers et al, 2004)
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