Abstract
The dual-targeted mitochondrial and chloroplastic zinc metallooligopeptidase from Arabidopsis, AtPreP, functions as a peptidasome that degrades targeting peptides and other small unstructured peptides. In addition to Zn located in the catalytic site, AtPreP also contains two Mg-binding sites. We have investigated the role of Mg-binding using AtPreP variants, in which one or both sites were rendered unable to bind Mg2+. Our results show that metal binding besides that of the active site is crucial for AtPreP proteolysis, particularly the inner site appears essential for normal proteolytic function. This is also supported by its evolutionary conservation among all plant species of PreP. Structured summaryMINT-7231937, MINT-7232017, MINT-7232035, MINT-7232051, MINT-7232070, MINT-7232090:AtPreP1 (uniprotkb:Q9LJL3) enzymaticly reacts (MI:0414) pF1 beta (uniprotkb:P17614) by protease assay (MI:0435)MINT-7232132:AtPreP1 (uniprotkb:Q9LJL3) enzymaticly reacts (MI:0414) galanin (uniprotkb:P22466) by protease assay (MI:0435)MINT-7232175:AtPreP1 (uniprotkb:Q9LJL3) enzymaticly reacts (MI:0414) Cecropin A (uniprotkb:P14954) by protease assay (MI:0435)MINT-7232163:AtPreP1 (uniprotkb:Q9LJL3) enzymaticly reacts (MI:0414) hPrPss (uniprotkb:P04156) by protease assay (MI:0435)
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