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Chararcterization of the targeting signal of dual-targeted pea glutathione reductase
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2003 In: Plant molecular biology, ISSN 0167-4412, Vol. 53, 341-356 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2003. Vol. 53, 341-356 p.
URN: urn:nbn:se:su:diva-23726OAI: diva2:194196
Part of urn:nbn:se:su:diva-462Available from: 2005-04-26 Created: 2005-04-26Bibliographically approved
In thesis
1. Dual targeting of glutathione reductase to mitochondria and chloroplasts
Open this publication in new window or tab >>Dual targeting of glutathione reductase to mitochondria and chloroplasts
2005 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

As a consequence of the presence of both mitochondria and chloroplasts in plant cells there is a higher sorting requirement in a plant cell than that in a non-plant cell. Reflecting this, protein import to mitochondria and chloroplasts has been shown to be highly specific. However, there is a group of proteins which are encoded by a single gene in the nucleus, translated in the cytosol and targeted to both mitochondria and chloroplasts. These proteins are referred to as dual targeted proteins. The first protein shown to be dual targeted was pea glutathione reductase (GR). The focus of this thesis is the targeting properties of the dual targeted protein glutathione reductase.

In order to overcome the limitations with traditional in vitro import systems we have developed an import system for simultaneous import of precursor proteins into mitochondria and chloroplasts (dual import system). The chloroplastic precursor of the small subunit of ribulose bisphosphate carboxylase/oxygenase (SSU) was mis-targeted to pea mitochondria in a single import system, but was imported only into chloroplasts in the dual system. The dual GR reductase precursor was targeted to both mitochondria and chloroplasts in both the single and dual import system.

We have investigated the targeting and processing properties of the GR targeting signal. Using N-terminal truncations we have demonstrated that the GR targeting signal has a domain organisation. Our results show that GR has evolved a dual targeting signal with the C-terminal part being sufficient for chloroplast import, the internal part required for the mitochondrial import and the N-terminal part housing a “fine-tuning” function. Furthermore, we have constructed a range of point mutations on the GR signal sequence changing positive amino acid residues and stretches of hydrophobic amino acid residues. Overall single mutations had a greater effect on mitochondrial import compared to import into chloroplasts. We have also shown that the recognition of the GR processing site differs between MPP and SPP. Single amino acid substitutions in the vicinity of the processing site clearly affected processing by MPP while processing by SPP showed low sensitivity to single mutations.

Place, publisher, year, edition, pages
Stockholm: Institutionen för biokemi och biofysik, 2005
dual targeting, mitochondria, chloroplasts, import
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
urn:nbn:se:su:diva-462 (URN)91-7155-019-4 (ISBN)
Public defence
2005-05-27, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 12 A, Stockholm, 10:00
Available from: 2005-04-26 Created: 2005-04-26Bibliographically approved

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