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The role of the N-terminal domain of chloroplast targeting peptides in organellar protein import and miss-sorting
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. (E. Glaser)
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. (E. Glaser)
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. (E. Glaser)
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. (E. Glaser)
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2006 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 580, no 16, 3966-3972 p.Article in journal (Refereed) Published
Abstract [en]

We have analysed 385 mitochondrial and 567 chloroplastic signal sequences of proteins found in the organellar proteomes of Arabidopsis thaliana. Despite overall similarities, the first 16 residues of transit peptides differ remarkably. To test the hypothesis that the N-terminally truncated transit peptides would redirect chloroplastic precursor proteins to mitochondria, we studied import of the N-terminal deletion mutants of ELIP, PetC and Lhcb2.1. The results show that the deletion mutants were neither imported into chloroplasts nor miss-targeted to mitochondria in vitro and in vivo, showing that the entire transit peptide is necessary for correct targeting as well as miss-sorting.

Place, publisher, year, edition, pages
2006. Vol. 580, no 16, 3966-3972 p.
Keyword [en]
Chloroplast; Mitochondria; Targeting peptide; Protein import; Miss-sorting
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:su:diva-8750DOI: 10.1016/j.febslet.2006.06.018PubMedID: 16806197OAI: oai:DiVA.org:su-8750DiVA: diva2:175269
Available from: 2007-12-21 Created: 2007-12-21 Last updated: 2017-12-13Bibliographically approved
In thesis
1. Dual Targeting of Proteins to Mitochondria and Chloroplasts
Open this publication in new window or tab >>Dual Targeting of Proteins to Mitochondria and Chloroplasts
2009 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The vast majority of mitochondrial and chloroplastic proteins are nuclear encoded, synthesized in the cytosol and imported into the respective organelle using an N-terminal extension, the targeting peptide (TP). After import into the organelle, the TP is cleaved off and degraded by the Presequence protease (PreP). The import process is thought to be highly specific, however there is a group of proteins that are localised to both mitochondria and chloroplasts, using an ambiguous, dual targeting peptide (dTP). The aim of this thesis was to investigate targeting properties of dTPs. Analysis of the amino acid content of all currently known dually targeted proteins revealed that the dTPs are enriched in hydroxylated, hydrophobic and positively charged residues, lacking acidic residues, whereas the content of serine, arginine and proline is intermediary in comparison to the mitochondrial and chloroplastic TPs. dTPs do not form amphiphilic a-helices, characteristic of the mitochondrial TPs, but the helical structure can be induced in membrane mimetic environment, as revealed by spectroscopic studies of a dTP of an aminoacyl- tRNA-synthetase (aaRS). In vitro and in vivo import experiments of fusion constructs containing N-terminal truncations of seven aaRS-dTPs coupled to green fluorescent protein (GFP) demonstrated different organisation of targeting determinants showing that the N-terminal portion of dTPs was crucial for import into both organelles or at least one organelle for different constructs. In addition, studies of targeting capacity of the TPs of PreP homologues from plant, mammal and yeast (AtPreP, hPreP and Mop112) showed species dependent intra-mitochondrial localisation of the coupled GFP and demonstrated functional complementation of an intermembrane space located Mop112 with a matrix located AtPreP. The studies presented here contribute to understanding of the intracellular and intra-mitochondrial sorting process of proteins in the eukaryotic cell.

Place, publisher, year, edition, pages
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2009. 74 p.
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Research subject
Biochemistry
Identifiers
urn:nbn:se:su:diva-31048 (URN)978-91-7155-971-5 (ISBN)
Public defence
2009-12-17, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 13:00 (English)
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Note
At the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 4: Manuscript.Available from: 2009-11-25 Created: 2009-11-02 Last updated: 2009-11-04Bibliographically approved

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