Interplay between N-terminal methionine excision and FtsH protease is essential for normal chloroplast development and function in Arabidopsis
| Autor: | Frédéric Frottin, Thierry Meinnel, Zach Adam, Carmela Giglione, Christelle Espagne |
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| Přispěvatelé: | Institut des sciences du végétal (ISV), Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
0106 biological sciences
Chlorophyll MESH: Amidohydrolases Chloroplasts Light medicine.medical_treatment Arabidopsis Plant Science 01 natural sciences Thylakoids Methionine MESH: Thylakoids ATP-Dependent Proteases Protein biosynthesis Arabidopsis thaliana MESH: Arabidopsis Research Articles 0303 health sciences medicine.diagnostic_test biology MESH: Photosystem II Protein Complex Chloroplast MESH: Plant Leaves Phenotype Biochemistry MESH: Protein Biosynthesis MESH: Membrane Proteins MESH: Chlorophyll Proteases Proteolysis MESH: Proteolysis MESH: Arabidopsis Proteins Protein degradation MESH: Phenotype Models Biological Amidohydrolases 03 medical and health sciences MESH: ATP-Dependent Proteases medicine [SDV.BV]Life Sciences [q-bio]/Vegetal Biology 030304 developmental biology Protease MESH: Chloroplasts Arabidopsis Proteins MESH: Models Biological Membrane Proteins Photosystem II Protein Complex Cell Biology biology.organism_classification MESH: Light Plant Leaves Mutagenesis Insertional MESH: Mutagenesis Insertional Seedlings Protein Biosynthesis MESH: Protein Processing Post-Translational MESH: Methionine MESH: Seedling Protein Processing Post-Translational 010606 plant biology & botany |
| Zdroj: | The Plant cell The Plant cell, American Society of Plant Biologists (ASPB), 2011, 23 (10), pp.3745-60. ⟨10.1105/tpc.111.087239⟩ |
| ISSN: | 1040-4651 1532-298X |
| DOI: | 10.1105/tpc.111.087239⟩ |
| Popis: | N-terminal methionine excision (NME) is the earliest modification affecting most proteins. All compartments in which protein synthesis occurs contain dedicated NME machinery. Developmental defects induced in Arabidopsis thaliana by NME inhibition are accompanied by increased proteolysis. Although increasing evidence supports a connection between NME and protein degradation, the identity of the proteases involved remains unknown. Here we report that chloroplastic NME (cNME) acts upstream of the FtsH protease complex. Developmental defects and higher sensitivity to photoinhibition associated with the ftsh2 mutation were abolished when cNME was inhibited. Moreover, the accumulation of D1 and D2 proteins of the photosystem II reaction center was always dependent on the prior action of cNME. Under standard light conditions, inhibition of chloroplast translation induced accumulation of correctly NME-processed D1 and D2 in a ftsh2 background, implying that the latter is involved in protein quality control, and that correctly NME-processed D1 and D2 are turned over primarily by the thylakoid FtsH protease complex. By contrast, inhibition of cNME compromises the specific N-terminal recognition of D1 and D2 by the FtsH complex, whereas the unprocessed forms are recognized by other proteases. Our results highlight the tight functional interplay between NME and the FtsH protease complex in the chloroplast. |
| Databáze: | OpenAIRE |
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