Discrete mutations in the presequence of potato formate dehydrogenase inhibit the in vivo targeting of GFP fusions into mitochondria
| Autor: | Catherine Colas des Francs-Small, Olivier Grandjean, Françoise Ambard-Bretteville, Ian Small |
|---|---|
| Přispěvatelé: | Unité de recherche en génomique végétale (URGV), Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE)-Institut National de la Recherche Agronomique (INRA), Unité de recherche Génétique et amélioration des plantes (GAP), Institut National de la Recherche Agronomique (INRA), ProdInra, Migration, Institut National de la Recherche Agronomique (INRA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Green Fluorescent Proteins
Molecular Sequence Data Biophysics Mitochondrion Biology Formate dehydrogenase Biochemistry Green fluorescent protein Structure-Activity Relationship In vivo Tobacco medicine [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Functional studies Molecular Biology Mitochondrial protein ComputingMilieux_MISCELLANEOUS Solanum tuberosum DICOTYLEDONES Cell Biology Formate Dehydrogenases Recombinant Proteins Mitochondria Plant Leaves Luminescent Proteins Protein Transport Cytosol medicine.anatomical_structure Mutagenesis Site-Directed Nucleus |
| Zdroj: | Biochemical and Biophysical Research Communications Biochemical and Biophysical Research Communications, Elsevier, 2003, 311, pp.966-971 Biochemical and Biophysical Research Communications, 2003, 311, pp.966-971 |
| ISSN: | 0006-291X 1090-2104 |
| Popis: | Most mitochondrial proteins are encoded by the nucleus, translated in the cytosol, and imported. Mitochondrial precursors generally contain their targeting information in a cleavable N-terminal presequence, which is rich in hydroxylated and positively charged residues and can form amphiphilic alpha-helices. We report the in vivo targeting of green fluorescent protein (GFP) by the FDH presequence, as well as several truncated or mutated variants. Some of these mutations modify the amphiphilicity of the predicted alpha-helix. The removal of the first two residues abolishes import and some single amino acid mutations strongly inhibit import. Such strong effects on import had not been observed in similar studies on other plant mitochondrial presequences, suggesting that the FDH presequence is a particularly good model for functional studies. |
| Databáze: | OpenAIRE |
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