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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Two novel mitochondrial and chloroplastic targeting-peptide-degrading peptidasomes in A. thaliana, AtPreP1 and AtPreP2

Elzbieta Glaser
  • Department for Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Stefan Nilsson
  • Department for Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Shashi Bhushan
  • Department for Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-11-02 | DOI: https://doi.org/10.1515/BC.2006.180

Abstract

Two novel metalloendopeptidases in Arabidopsis thaliana, AtPreP1 and AtPreP2, are responsible for the degradation of targeting peptides in mitochondria and chloroplasts. Both AtPreP1 and AtPreP2 contain ambiguous targeting peptides and are dually targeted to both organelles. The proteases also have the capacity to degrade unstructured peptides of up to 65 amino acid residues, but not small proteins. The catalysis occurs in a huge catalytic chamber revealed by the crystal structure of AtPreP1 at 2.1 Å. The enzymes show a preference for basic and small uncharged amino acids or serines at the cleavage sites. Despite similarities in cleavage specificities, cleavage-site recognition differs for both proteases and is context- and structure-dependent. The AtPreP1 and AtPreP2 genes are differentially expressed in Arabidopsis.

Keywords: chloroplast; mitochondria; peptidase; protease; protein import; targeting peptide; transit peptide

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Published Online: 2006-11-02

Published in Print: 2006-10-01


Citation Information: Biological Chemistry, Volume 387, Issue 10/11, Pages 1441–1447, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.180.

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