Intraplastidial trafficking of a phage-type RNA polymerase is mediated by a thylacoïd RING-H2 protein
| Autor: | Silva Lerbs-Mache, Thierry Lagrange, Mohamed-Ali Hakimi, Pankaj Jaiswal, Florence Courtois, Emilie Demarsy, Laurence Maréchal-Drouard, Jacinthe Azevedo, Jean-Pierre Alcaraz |
|---|---|
| Přispěvatelé: | Institut de biologie moléculaire des plantes (IBMP), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Plastes et différenciation cellulaire (PDC), Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Laboratoire Adaptation et pathogénie des micro-organismes [Grenoble] (LAPM), Center for Integrative Genomics - Institute of Bioinformatics, Génopode (CIG), Swiss Institute of Bioinformatics [Lausanne] (SIB), Université de Lausanne (UNIL)-Université de Lausanne (UNIL), Laboratoire Génome et développement des plantes (LGDP), Université de Perpignan Via Domitia (UPVD)-Centre National de la Recherche Scientifique (CNRS), Department of Plant Breeding and Genetics, Cornell University [New York], Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
0106 biological sciences
Light Arabidopsis MESH: Amino Acid Sequence Thylakoids 01 natural sciences chemistry.chemical_compound MESH: Saccharomyces cerevisiae Proteins MESH: Thylakoids Gene Expression Regulation Plant Transcription (biology) RNA Ribosomal 16S RNA polymerase MESH: Arabidopsis Bacteriophages Promoter Regions Genetic MESH: Organ Specificity 0303 health sciences Multidisciplinary food and beverages MESH: Transcription Factors DNA-Directed RNA Polymerases Biological Sciences Transport protein Cell biology MESH: RNA Ribosomal 16S DNA-Binding Proteins Chloroplast MESH: Promoter Regions (Genetics) MESH: Intracellular Membranes Protein Transport Transmembrane domain Organ Specificity Thylakoid Protein Binding MESH: Protein Transport Saccharomyces cerevisiae Proteins Molecular Sequence Data MESH: Arabidopsis Proteins [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology MESH: Two-Hybrid System Techniques DNA-binding protein 03 medical and health sciences Two-Hybrid System Techniques MESH: Gene Library MESH: Protein Binding [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology MESH: Bacteriophages Amino Acid Sequence RNA Messenger MESH: Gene Expression Regulation Plant Plastid MESH: RNA Messenger Gene Library 030304 developmental biology MESH: Molecular Sequence Data Arabidopsis Proteins Intracellular Membranes Molecular biology MESH: Light MESH: DNA-Directed RNA Polymerases chemistry Transcription Factors 010606 plant biology & botany |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2008, 105, pp.9123-9128 Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2008, 105 (26), pp.9123-8. ⟨10.1073/pnas.0800909105⟩ |
| ISSN: | 0027-8424 1091-6490 |
| DOI: | 10.1073/pnas.0800909105⟩ |
| Popis: | The plastid genome of dicotyledonous plants is transcribed by three different RNA polymerases; an eubacterial-type enzyme, PEP; and two phage-type enzymes, RPOTp and RPOTmp. RPOTp plays an important role in chloroplast transcription, biogenesis, and mesophyll cell proliferation. RPOTmp fulfills a specific function in the transcription of the rrn operon in proplasts/amyloplasts during seed imbibition/germination and a more general function in chloroplasts during later developmental stages. In chloroplasts, RPOTmp is tightly associated with thylakoid membranes indicating that functional switching of RPOTmp is connected to thylakoid association. By using the yeast two-hybrid system, we have identified two proteins that interact with RPOTmp. The two proteins are very similar, both characterized by three N-terminal transmembrane domains and a C-terminal RING domain. We show that at least one of these proteins is an intrinsic thylakoid membrane protein that fixes RPOTmp on the stromal side of the thylakoid membrane, probably via the RING domain. A model is presented in which light by triggering the synthesis of the RING protein determines membrane association and functional switching of RPOTmp. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|