Binding of divalent cations is essential for the activity of the organellar peptidasome in Arabidopsis thaliana, AtPreP.

Full 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 Mg(2+). 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.

Author information

Author/s: Bäckman, Hans G (HG); Pessoa, João (J); Eneqvist, Therese (T); Glaser, Elzbieta (E);

Affiliation: Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: FEBS letters (FEBS Lett), published in Netherlands. (Language: eng)

Reference: 2009-Sep; vol 583 (issue 17) : pp 2727-33

Dates: Created 2009/09/01; Completed 2009/10/22;

PMID: 19646442, status: MEDLINE (last retrieval date: 10/22/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Amino Acid Sequence
Animals
Arabidopsis - genetics; metabolism
Arabidopsis Proteins - chemistry; genetics; metabolism
Catalytic Domain
Cations, Divalent - metabolism
Crystallography, X-Ray
Humans
Models, Molecular

Models, Molecular
Molecular Sequence Data
Organelles - enzymology
Peptide Hydrolases - chemistry; genetics; metabolism
Plant Proteins - chemistry; genetics; metabolism
Point Mutation
Protein Isoforms - chemistry; genetics; metabolism
Protein Structure, Tertiary
Sequence Alignment

Associated Chemicals: Arabidopsis Proteins (0) ; Cations, Divalent (0) ; Plant Proteins (0) ; Protein Isoforms (0) ; Peptide Hydrolases (EC 3.4.-) ; presequence protease PreP, Arabidopsis (EC 3.4.-)

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