Change search
ReferencesLink to record
Permanent link

Direct link
The organellar peptidasome, PreP: a journey from Arabidopsis to Alzheimer's disease
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2010 (English)In: Biochimica et Biophysica Acta, ISSN 0006-3002, Vol. 1797, no 6-7, 1076-80 p.Article in journal (Refereed) Published
Abstract [en]

The novel peptidasome, called presequence protease, PreP, was originally identified and characterized in Arabidopsis thaliana as a mitochondrial matrix and chloroplast stroma localized metalloprotease. PreP has a function as the organellar peptide clearing protease and is responsible for degrading free targeting peptides and also other unstructured peptides up to 65 amino acid residues that might be toxic to organellar functions. PreP contains an inverted Zn-binding motif and belongs to the pitrilysin protease family. The crystal structure of AtPreP refined at 2.1 A demonstrated a unique totally enclosed large cavity of 10000 A3 that opens and closes in response to peptide binding, revealing a novel catalytic mechanism for proteolysis. Homologues of PreP have been found in yeast and human mitochondria. Interestingly, the human PreP, hPreP, is the protease that is responsible for clearing the human brain mitochondria from the toxic amyloid-beta peptide (Abeta) associated with Alzheimer's disease (AD). Accumulation of Abeta has been shown in the brain mitochondria from AD patients and mutant transgenic mice overexpressing Abeta. Here, we present a review of our present knowledge on structural and functional characteristics of PreP and discuss its mitochondrial Abeta-degrading activity in the human brain mitochondria in relation to AD.

Place, publisher, year, edition, pages
2010. Vol. 1797, no 6-7, 1076-80 p.
Keyword [en]
Mitochondria; Presequence protease; Peptide degradation; Amyloid-β peptide; Alzheimer's disease; Targeting peptide
National Category
Natural Sciences
Research subject
Biophysics; Biochemistry
URN: urn:nbn:se:su:diva-51711DOI: 10.1016/j.bbabio.2009.12.016PubMedID: 20036633OAI: diva2:385738
Available from: 2011-01-12 Created: 2011-01-12 Last updated: 2011-02-17Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Glaser, ElzbietaAlikhani, Nyosha
By organisation
Department of Biochemistry and Biophysics
In the same journal
Biochimica et Biophysica Acta
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 23 hits
ReferencesLink to record
Permanent link

Direct link