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A novel mitochondrial and chloroplast peptidasome, PreP
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2012 (English)In: Physiologia Plantarum: An International Journal for Plant Biology, ISSN 0031-9317, E-ISSN 1399-3054, Vol. 145, no 1, 180-186 p.Article in journal (Refereed) Published
Abstract [en]

A novel mitochondrial and chloroplast peptidasome, the Presequence Protease (PreP) degrades organellar targeting peptides as well as other unstructured peptides up to 65 amino acid residues in length. PreP belongs to the pitrilysin oligopeptidase family (M16C) containing an inverted zinc-binding motif. The crystal structure of Arabidopsis thaliana PreP, AtPreP, refined at 2.1 angstrom, revealed a novel mechanism of proteolysis in which two halves of the enzyme connected by a hinge region enclose a large catalytic chamber opening and closing in response to peptide binding. Double knock-out mutant of AtPreP1 and AtPreP2 results in a severe phenotype, including decreased size and growth rate, chlorosis and organellar abnormalities, such as altered chloroplast starch content, partial loss of the integrity of the inner mitochondrial membrane and reduced mitochondrial respiration. PreP homologues are also present in yeast and humans. Interestingly, human PreP has been associated with Alzheimer's disease as it is responsible for degradation of amyloid-beta peptide in brain mitochondria.

Place, publisher, year, edition, pages
2012. Vol. 145, no 1, 180-186 p.
National Category
Plant Biotechnology
Identifiers
URN: urn:nbn:se:su:diva-80769DOI: 10.1111/j.1399-3054.2011.01531.xISI: 000302802900018OAI: oai:DiVA.org:su-80769DiVA: diva2:557626
Note

AuthorCount:2;

Available from: 2012-09-28 Created: 2012-09-27 Last updated: 2017-12-07Bibliographically approved

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Kmiec-Wisniewska, BeataGlaser, Elzbieta
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