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- Title
Binding of divalent cations is essential for the activity of the organellar peptidasome in Arabidopsis thaliana, AtPreP
- Authors
Bäckman, Hans G.; Pessoa, João; Eneqvist, Therese; Glaser, Elzbieta
- Abstract
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 summary: MINT-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)
- Subjects
PROTEIN binding; CATIONS; ARABIDOPSIS thaliana; GENE targeting; PEPTIDASE; ORGANELLES; PEPTIDES; CELL physiology
- Publication
FEBS Letters, 2009, Vol 583, Issue 17, p2727
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.07.040