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[PMID]:27742488
[Au] Autor:Bujaldon S; Kodama N; Rappaport F; Subramanyam R; de Vitry C; Takahashi Y; Wollman FA
[Ad] Endereço:Institut de Biologie Physico-Chimique, UMR7141 CNRS-UPMC, Paris 75005, France.
[Ti] Título:Functional Accumulation of Antenna Proteins in Chlorophyll b-Less Mutants of Chlamydomonas reinhardtii.
[So] Source:Mol Plant;10(1):115-130, 2017 Jan 09.
[Is] ISSN:1752-9867
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The green alga Chlamydomonas reinhardtii contains several light-harvesting chlorophyll a/b complexes (LHC): four major LHCIIs, two minor LHCIIs, and nine LHCIs. We characterized three chlorophyll b-less mutants to assess the effect of chlorophyll b deficiency on the function, assembly, and stability of these chlorophyll a/b binding proteins. We identified point mutations in two mutants that inactivate the CAO gene responsible for chlorophyll a to chlorophyll b conversion. All LHCIIs accumulated to wild-type levels in a CAO mutant but their light-harvesting function for photosystem II was impaired. In contrast, most LHCIs accumulated to wild-type levels in the mutant and their light-harvesting capability for photosystem I remained unaltered. Unexpectedly, LHCI accumulation and the photosystem I functional antenna size increased in the mutant compared with in the wild type when grown in dim light. When the CAO mutation was placed in a yellow-in-the-dark background (yid-BF3), in which chlorophyll a synthesis remains limited in dim light, accumulation of the major LHCIIs and of most LHCIs was markedly reduced, indicating that sustained synthesis of chlorophyll a is required to preserve the proteolytic resistance of antenna proteins. Indeed, after crossing yid-BF3 with a mutant defective for the thylakoid FtsH protease activity, yid-BF3-ftsh1 restored wild-type levels of LHCI, which defines LHCI as a new substrate for the FtsH protease.
[Mh] Termos MeSH primário: Chlamydomonas reinhardtii/metabolismo
Proteínas de Ligação à Clorofila/metabolismo
Clorofila/fisiologia
[Mh] Termos MeSH secundário: Alelos
Chlamydomonas reinhardtii/genética
Chlamydomonas reinhardtii/efeitos da radiação
Clorofila/biossíntese
Clorofila/genética
Proteínas de Ligação à Clorofila/genética
Luz
Oxigenases/metabolismo
Mutação Puntual
Proteínas das Membranas dos Tilacoides/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chlorophyll Binding Proteins); 0 (Thylakoid Membrane Proteins); 1406-65-1 (Chlorophyll); 5712ZB110R (chlorophyll b); EC 1.13.- (Oxygenases); EC 1.13.12.- (chlorophyll a oxygenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161016
[St] Status:MEDLINE


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[PMID]:27702692
[Au] Autor:Wang F; Qi Y; Malnoë A; Choquet Y; Wollman FA; de Vitry C
[Ad] Endereço:Institut de Biologie Physico-Chimique, Unité Mixte de Recherche 7141, Centre National de la Recherche Scientifique/Université Pierre et Marie Curie, Paris 75005, France.
[Ti] Título:The High Light Response and Redox Control of Thylakoid FtsH Protease in Chlamydomonas reinhardtii.
[So] Source:Mol Plant;10(1):99-114, 2017 Jan 09.
[Is] ISSN:1752-9867
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In Chlamydomonas reinhardtii, the major protease involved in the maintenance of photosynthetic machinery in thylakoid membranes, the FtsH protease, mostly forms large hetero-oligomers (∼1 MDa) comprising FtsH1 and FtsH2 subunits, whatever the light intensity for growth. Upon high light exposure, the FtsH subunits display a shorter half-life, which is counterbalanced by an increase in FTSH1/2 mRNA levels, resulting in the modest upregulation of FtsH1/2 proteins. Furthermore, we found that high light increases the protease activity through a hitherto unnoticed redox-controlled reduction of intermolecular disulfide bridges. We isolated a Chlamydomonas FTSH1 promoter-deficient mutant, ftsh1-3, resulting from the insertion of a TOC1 transposon, in which the high light-induced upregulation of FTSH1 gene expression is largely lost. In ftsh1-3, the abundance of FtsH1 and FtsH2 proteins are loosely coupled (decreased by 70% and 30%, respectively) with no formation of large and stable homo-oligomers. Using strains exhibiting different accumulation levels of the FtsH1 subunit after complementation of ftsh1-3, we demonstrate that high light tolerance is tightly correlated with the abundance of the FtsH protease. Thus, the response of Chlamydomonas to light stress involves higher levels of FtsH1/2 subunits associated into large complexes with increased proteolytic activity.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Chlamydomonas reinhardtii/metabolismo
Luz
Metaloproteases/metabolismo
Proteínas das Membranas dos Tilacoides/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Chlamydomonas reinhardtii/genética
Chlamydomonas reinhardtii/efeitos da radiação
Metaloproteases/genética
Oxirredução
Regiões Promotoras Genéticas
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Proteólise
Supressão Genética
Proteínas das Membranas dos Tilacoides/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Protein Isoforms); 0 (Thylakoid Membrane Proteins); EC 3.4.- (Metalloproteases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161006
[St] Status:MEDLINE


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[PMID]:27555564
[Au] Autor:Zhan J; Zhu X; Zhou W; Chen H; He C; Wang Q
[Ad] Endereço:Key Laboratory of Algal Biology, Institute of Hydrobiology, the Chinese Academy of Sciences, Wuhan, Hubei, 430072, China.
[Ti] Título:Thf1 interacts with PS I and stabilizes the PS I complex in Synechococcus sp. PCC7942.
[So] Source:Mol Microbiol;102(4):738-751, 2016 11.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Thylakoid formation1 protein (Thf1) is a multifunctional protein that is conserved in all photosynthetic organisms. In this study, we used the model cyanobacterium Synechococcus sp. PCC7942 (hereafter Synechococcus) to show that the level of Thf1 is altered in response to various stress conditions. Although this protein has been reported to be involved in thylakoid formation, the thylakoid membrane in the thf1 deletion strain (ΔThf1) was not affected. Compared with the WT, ΔThf1 showed reduced PS II activity, with increased levels of D1 under high light (HL) conditions, which was resulted from blocked D1 degradation by the FtsH protease and thus inhibits PS II repair. PS I was found to be more seriously affected than PS II in ΔThf1, even under low light conditions, suggesting that PS I damage could be the primary effect of thf1 deletion in Synechococcus. Further analysis revealed that the ΔThf1 mutant had a lower PS I subunit content and lower PS I stability under HL conditions. Further sucrose gradient fractionation of the membrane protein complexes and crosslinking and immunoblot analysis indicated that Thf1 interacts with PS I. Together, our results reveal that Thf1 interacts with PS I and thereby stabilizes PS I in Synechococcus.
[Mh] Termos MeSH primário: Complexo de Proteína do Fotossistema I/metabolismo
Synechococcus/metabolismo
Proteínas das Membranas dos Tilacoides/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Luz
Fotossíntese
Complexo de Proteína do Fotossistema II/metabolismo
Tilacoides/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Photosystem I Protein Complex); 0 (Photosystem II Protein Complex); 0 (Thylakoid Membrane Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160825
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13488


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[PMID]:27493208
[Au] Autor:Sautron E; Giustini C; Dang T; Moyet L; Salvi D; Crouzy S; Rolland N; Catty P; Seigneurin-Berny D
[Ad] Endereço:From the CNRS, Laboratoire de Physiologie Cellulaire et Végétale, UMR 5168, F-38054 Grenoble, France, the Université Grenoble Alpes, F-38054 Grenoble, France, the CEA, DSV, BIG, F-38054 Grenoble, France, the INRA, LPCV, UMR 1417, F-38054 Grenoble, France, and.
[Ti] Título:Identification of Two Conserved Residues Involved in Copper Release from Chloroplast PIB-1-ATPases.
[So] Source:J Biol Chem;291(38):20136-48, 2016 Sep 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Copper is an essential transition metal for living organisms. In the plant model Arabidopsis thaliana, half of the copper content is localized in the chloroplast, and as a cofactor of plastocyanin, copper is essential for photosynthesis. Within the chloroplast, copper delivery to plastocyanin involves two transporters of the PIB-1-ATPases subfamily: HMA6 at the chloroplast envelope and HMA8 in the thylakoid membranes. Both proteins are high affinity copper transporters but share distinct enzymatic properties. In the present work, the comparison of 140 sequences of PIB-1-ATPases revealed a conserved region unusually rich in histidine and cysteine residues in the TMA-L1 region of eukaryotic chloroplast copper ATPases. To evaluate the role of these residues, we mutated them in HMA6 and HMA8. Mutants of interest were selected from phenotypic tests in yeast and produced in Lactococcus lactis for further biochemical characterizations using phosphorylation assays from ATP and Pi Combining functional and structural data, we highlight the importance of the cysteine and the first histidine of the CX3HX2H motif in the process of copper release from HMA6 and HMA8 and propose a copper pathway through the membrane domain of these transporters. Finally, our work suggests a more general role of the histidine residue in the transport of copper by PIB-1-ATPases.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/química
Proteínas de Arabidopsis/química
Arabidopsis/enzimologia
Cobre/química
Proteínas das Membranas dos Tilacoides/química
Tilacoides/enzimologia
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Motivos de Aminoácidos
Arabidopsis/genética
Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Cobre/metabolismo
Histidina/química
Histidina/genética
Histidina/metabolismo
Lactococcus lactis/genética
Lactococcus lactis/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas das Membranas dos Tilacoides/genética
Proteínas das Membranas dos Tilacoides/metabolismo
Tilacoides/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (HMA8 protein, Arabidopsis); 0 (Recombinant Proteins); 0 (Thylakoid Membrane Proteins); 4QD397987E (Histidine); 789U1901C5 (Copper); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (HMA6 protein, Arabidopsis)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170916
[Lr] Data última revisão:
170916
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160806
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.706978


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[PMID]:27439459
[Au] Autor:van Buer J; Cvetkovic J; Baier M
[Ad] Endereço:Dahlem Center of Plant Sciences, Plant Physiology, Freie Universität Berlin, Königin-Luise-Straße 12-16, 14195, Berlin, Germany.
[Ti] Título:Cold regulation of plastid ascorbate peroxidases serves as a priming hub controlling ROS signaling in Arabidopsis thaliana.
[So] Source:BMC Plant Biol;16(1):163, 2016 Jul 20.
[Is] ISSN:1471-2229
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Short cold periods comprise a challenge to plant growth and development. Series of cold stresses improve plant performance upon a future cold stress. This effect could be provoked by priming, training or acclimation dependent hardening. Here, we compared the effect of 24 h (short priming stimulus) and of 2 week long cold-pretreatment (long priming stimulus) on the response of Arabidopsis thaliana to a single 24 h cold stimulus (triggering) after a 5 day long lag-phase, to test Arabidopsis for cold primability. RESULTS: Three types of pretreatment dependent responses were observed: (1) The CBF-regulon controlled gene COR15A was stronger activated only after long-term cold pretreatment. (2) The non-chloroplast specific stress markers PAL1 and CHS were more induced by cold after long-term and slightly stronger expressed after short-term cold priming. (3) The chloroplast ROS signaling marker genes ZAT10 and BAP1 were less activated by the triggering stimulus in primed plants. The effects on ZAT10 and BAP1 were more pronounced in 24 h cold-primed plants than in 14 day long cold-primed ones demonstrating independence of priming from induction and persistence of primary cold acclimation responses. Transcript and protein abundance analysis and studies in specific knock-out lines linked the priming-specific regulation of ZAT10 and BAP1 induction to the priming-induced long-term regulation of stromal and thylakoid-bound ascorbate peroxidase (sAPX and tAPX) expression. CONCLUSION: The plastid antioxidant system, especially, plastid ascorbate peroxidase regulation, transmits information on a previous cold stress over time without the requirement of establishing cold-acclimation. We hypothesize that the plastid antioxidant system serves as a priming hub and that priming-dependent regulation of chloroplast-to-nucleus ROS signaling is a strategy to prepare plants under unstable environmental conditions against unpredictable stresses by supporting extra-plastidic stress protection.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Ascorbato Peroxidases/metabolismo
Regulação da Expressão Gênica de Plantas
Plastídeos/enzimologia
Espécies Reativas de Oxigênio/metabolismo
Proteínas das Membranas dos Tilacoides/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Arabidopsis/metabolismo
Proteínas de Arabidopsis/genética
Ascorbato Peroxidases/genética
Proteínas de Cloroplastos/genética
Proteínas de Cloroplastos/metabolismo
Cloroplastos/enzimologia
Cloroplastos/genética
Cloroplastos/metabolismo
Temperatura Baixa
Estresse Oxidativo
Plastídeos/genética
Plastídeos/metabolismo
Proteínas das Membranas dos Tilacoides/genética
Tilacoides/enzimologia
Tilacoides/genética
Tilacoides/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (BON1-associated protein, Arabidopsis); 0 (COR15 protein, Arabidopsis); 0 (Chloroplast Proteins); 0 (Reactive Oxygen Species); 0 (Thylakoid Membrane Proteins); 0 (Zat10 protein, Arabidopsis); EC 1.11.1.11 (APXS protein, Arabidopsis); EC 1.11.1.11 (APXT protein, Arabidopsis); EC 1.11.1.11 (Ascorbate Peroxidases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160722
[St] Status:MEDLINE
[do] DOI:10.1186/s12870-016-0856-7


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[PMID]:27020959
[Au] Autor:Schneider A; Steinberger I; Herdean A; Gandini C; Eisenhut M; Kurz S; Morper A; Hoecker N; Rühle T; Labs M; Flügge UI; Geimer S; Schmidt SB; Husted S; Weber AP; Spetea C; Leister D
[Ad] Endereço:Molekularbiologie der Pflanzen (Botanik), Department Biologie I, Ludwig-Maximilians-Universität München, 82152 Martinsried, Germany anja.schneider@lrz.uni-muenchen.de.
[Ti] Título:The Evolutionarily Conserved Protein PHOTOSYNTHESIS AFFECTED MUTANT71 Is Required for Efficient Manganese Uptake at the Thylakoid Membrane in Arabidopsis.
[So] Source:Plant Cell;28(4):892-910, 2016 Apr.
[Is] ISSN:1532-298X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In plants, algae, and cyanobacteria, photosystem II (PSII) catalyzes the light-driven oxidation of water. The oxygen-evolving complex of PSII is a Mn4CaO5 cluster embedded in a well-defined protein environment in the thylakoid membrane. However, transport of manganese and calcium into the thylakoid lumen remains poorly understood. Here, we show that Arabidopsis thaliana PHOTOSYNTHESIS AFFECTED MUTANT71 (PAM71) is an integral thylakoid membrane protein involved in Mn(2+) and Ca(2+) homeostasis in chloroplasts. This protein is required for normal operation of the oxygen-evolving complex (as evidenced by oxygen evolution rates) and for manganese incorporation. Manganese binding to PSII was severely reduced in pam71 thylakoids, particularly in PSII supercomplexes. In cation partitioning assays with intact chloroplasts, Mn(2+) and Ca(2+) ions were differently sequestered in pam71, with Ca(2+) enriched in pam71 thylakoids relative to the wild type. The changes in Ca(2+) homeostasis were accompanied by an increased contribution of the transmembrane electrical potential to the proton motive force across the thylakoid membrane. PSII activity in pam71 plants and the corresponding Chlamydomonas reinhardtii mutant cgld1 was restored by supplementation with Mn(2+), but not Ca(2+) Furthermore, PAM71 suppressed the Mn(2+)-sensitive phenotype of the yeast mutant Δpmr1 Therefore, PAM71 presumably functions in Mn(2+) uptake into thylakoids to ensure optimal PSII performance.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Manganês/metabolismo
Proteínas das Membranas dos Tilacoides/metabolismo
Tilacoides/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Cálcio/metabolismo
Chlamydomonas reinhardtii/genética
Chlamydomonas reinhardtii/metabolismo
Cloroplastos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Thylakoid Membrane Proteins); 42Z2K6ZL8P (Manganese); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160330
[St] Status:MEDLINE
[do] DOI:10.1105/tpc.15.00812


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[PMID]:26951662
[Au] Autor:Liang FC; Kroon G; McAvoy CZ; Chi C; Wright PE; Shan SO
[Ad] Endereço:Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125;
[Ti] Título:Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release.
[So] Source:Proc Natl Acad Sci U S A;113(12):E1615-24, 2016 Mar 22.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Membrane protein biogenesis poses enormous challenges to cellular protein homeostasis and requires effective molecular chaperones. Compared with chaperones that promote soluble protein folding, membrane protein chaperones require tight spatiotemporal coordination of their substrate binding and release cycles. Here we define the chaperone cycle for cpSRP43, which protects the largest family of membrane proteins, the light harvesting chlorophyll a/b-binding proteins (LHCPs), during their delivery. Biochemical and NMR analyses demonstrate that cpSRP43 samples three distinct conformations. The stromal factor cpSRP54 drives cpSRP43 to the active state, allowing it to tightly bind substrate in the aqueous compartment. Bidentate interactions with the Alb3 translocase drive cpSRP43 to a partially inactive state, triggering selective release of LHCP's transmembrane domains in a productive unloading complex at the membrane. Our work demonstrates how the intrinsic conformational dynamics of a chaperone enables spatially coordinated substrate capture and release, which may be general to other ATP-independent chaperone systems.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/química
Arabidopsis/metabolismo
Proteínas de Cloroplastos/química
Complexos de Proteínas Captadores de Luz/metabolismo
Chaperonas Moleculares/metabolismo
Partícula de Reconhecimento de Sinal/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Arabidopsis/metabolismo
Sítios de Ligação
Proteínas de Cloroplastos/metabolismo
Proteínas de Membrana/metabolismo
Modelos Moleculares
Dados de Sequência Molecular
Ressonância Magnética Nuclear Biomolecular
Ligação Proteica
Conformação Proteica
Mapeamento de Interação de Proteínas
Estrutura Terciária de Proteína
Proteínas Recombinantes de Fusão/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Partícula de Reconhecimento de Sinal/metabolismo
Solubilidade
Relação Estrutura-Atividade
Proteínas das Membranas dos Tilacoides/metabolismo
Tilacoides/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ALBINO 3 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (Chloroplast Proteins); 0 (Light-Harvesting Protein Complexes); 0 (Membrane Proteins); 0 (Molecular Chaperones); 0 (Recombinant Fusion Proteins); 0 (Signal Recognition Particle); 0 (Thylakoid Membrane Proteins); 0 (cpSRP43 protein, Arabidopsis)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160309
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1524777113


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[PMID]:26944623
[Au] Autor:Klasek L; Inoue K
[Ad] Endereço:Department of Plant Sciences, University of California at Davis, Davis, CA, United States of America.
[Ti] Título:Dual Protein Localization to the Envelope and Thylakoid Membranes Within the Chloroplast.
[So] Source:Int Rev Cell Mol Biol;323:231-63, 2016.
[Is] ISSN:1937-6448
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The chloroplast houses various metabolic processes essential for plant viability. This organelle originated from an ancestral cyanobacterium via endosymbiosis and maintains the three membranes of its progenitor. Among them, the outer envelope membrane functions mainly in communication with cytoplasmic components while the inner envelope membrane houses selective transport of various metabolites and the biosynthesis of several compounds, including membrane lipids. These two envelope membranes also play essential roles in import of nuclear-encoded proteins and in organelle division. The third membrane, the internal membrane system known as the thylakoid, houses photosynthetic electron transport and chemiosmotic phosphorylation. The inner envelope and thylakoid membranes share similar lipid composition. Specific targeting pathways determine their defined proteomes and, thus, their distinct functions. Nonetheless, several proteins have been shown to exist in both the envelope and thylakoid membranes. These proteins include those that play roles in protein transport, tetrapyrrole biosynthesis, membrane dynamics, or transport of nucleotides or inorganic phosphate. In this review, we summarize the current knowledge about proteins localized to both the envelope and thylakoid membranes in the chloroplast, discussing their roles in each membrane and potential mechanisms of their dual localization. Addressing the unanswered questions about these dual-localized proteins should help advance our understanding of chloroplast development, protein transport, and metabolic regulation.
[Mh] Termos MeSH primário: Membrana Nuclear/metabolismo
Plantas/metabolismo
Proteínas das Membranas dos Tilacoides/metabolismo
Tilacoides/metabolismo
[Mh] Termos MeSH secundário: Membrana Nuclear/genética
Plantas/genética
Transporte Proteico/fisiologia
Proteínas das Membranas dos Tilacoides/genética
Tilacoides/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Thylakoid Membrane Proteins)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160306
[St] Status:MEDLINE


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[PMID]:26919668
[Au] Autor:Perello C; Llamas E; Burlat V; Ortiz-Alcaide M; Phillips MA; Pulido P; Rodriguez-Concepcion M
[Ad] Endereço:Program of Plant Metabolism and Metabolic Engineering, Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, 08193 Barcelona, Spain.
[Ti] Título:Differential Subplastidial Localization and Turnover of Enzymes Involved in Isoprenoid Biosynthesis in Chloroplasts.
[So] Source:PLoS One;11(2):e0150539, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plastidial isoprenoids are a diverse group of metabolites with roles in photosynthesis, growth regulation, and interaction with the environment. The methylerythritol 4-phosphate (MEP) pathway produces the metabolic precursors of all types of plastidial isoprenoids. Proteomics studies in Arabidopsis thaliana have shown that all the enzymes of the MEP pathway are localized in the plastid stroma. However, immunoblot analysis of chloroplast subfractions showed that the first two enzymes of the pathway, deoxyxylulose 5-phosphate synthase (DXS) and reductoisomerase (DXR), can also be found in non-stromal fractions. Both transient and stable expression of GFP-tagged DXS and DXR proteins confirmed the presence of the fusion proteins in distinct subplastidial compartments. In particular, DXR-GFP was found to accumulate in relatively large vesicles that could eventually be released from chloroplasts, presumably to be degraded by an autophagy-independent process. Together, we propose that protein-specific mechanisms control the localization and turnover of the first two enzymes of the MEP pathway in Arabidopsis chloroplasts.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Cloroplastos/enzimologia
Terpenos/metabolismo
[Mh] Termos MeSH secundário: Agrobacterium tumefaciens/genética
Aldose-Cetose Isomerases/genética
Aldose-Cetose Isomerases/metabolismo
Arabidopsis/ultraestrutura
Proteínas de Arabidopsis/genética
Cloroplastos/ultraestrutura
Genes Reporter
Vetores Genéticos/genética
Folhas de Planta/enzimologia
Folhas de Planta/ultraestrutura
Plantas Geneticamente Modificadas
Agregados Proteicos
Transporte Proteico
Proteínas Recombinantes de Fusão/metabolismo
Frações Subcelulares/enzimologia
Proteínas das Membranas dos Tilacoides/genética
Proteínas das Membranas dos Tilacoides/metabolismo
Tilacoides/metabolismo
Tabaco
Transferases/genética
Transferases/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Protein Aggregates); 0 (Recombinant Fusion Proteins); 0 (Terpenes); 0 (Thylakoid Membrane Proteins); EC 1.1.1.267 (1-deoxy-D-xylulose 5-phosphate reductoisomerase); EC 2.- (Transferases); EC 2.2.1.- (deoxyxylulose-5-phosphate synthase); EC 5.3.1.- (Aldose-Ketose Isomerases)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160227
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0150539


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[PMID]:26918860
[Au] Autor:Chen YE; Liu WJ; Su YQ; Cui JM; Zhang ZW; Yuan M; Zhang HY; Yuan S
[Ad] Endereço:College of Life Sciences, Sichuan Agricultural University, Ya'an 625014, China. anty9826@163.com.
[Ti] Título:Different response of photosystem II to short and long-term drought stress in Arabidopsis thaliana.
[So] Source:Physiol Plant;158(2):225-35, 2016 Oct.
[Is] ISSN:1399-3054
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:Short- and long-term drought stress on photosystem II (PSII) and oxidative stress were studied in Arabidopsis thaliana. Under drought stress, chlorophyll (Chl) content, Chl fluorescence, relative water content and oxygen evolution capacity gradually decreased, and the thylakoid structure was gradually damaged. Short-term drought stress caused a rapid disassembly of the light-harvesting complex II (LHCII). However, PSII dimers kept stable under the short-term drought stress and significantly decreased only after 15 days of drought stress. Immunoblotting analysis of the thylakoid membrane proteins showed that most of the photosystem proteins decreased after the stress, especially for Lhcb5, Lhcb6 and PsbQ proteins. However, surprisingly, PsbS significantly increased after the long-term drought stress, which is consistent with the substantially increased non-photochemical quenching (NPQ) after the stress. Our results suggest that the PSII-LHCII supercomplexes and LHCII assemblies play an important role in preventing photo-damages to PSII under drought stress.
[Mh] Termos MeSH primário: Arabidopsis/fisiologia
Complexos de Proteínas Captadores de Luz/metabolismo
Complexo de Proteína do Fotossistema II/metabolismo
Proteínas das Membranas dos Tilacoides/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/efeitos da radiação
Arabidopsis/ultraestrutura
Proteínas de Arabidopsis/metabolismo
Clorofila/metabolismo
Cloroplastos/metabolismo
Cloroplastos/ultraestrutura
Secas
Regulação da Expressão Gênica de Plantas
Luz
Peroxidação de Lipídeos
Estresse Oxidativo
Oxigênio/metabolismo
Fosforilação
Folhas de Planta/fisiologia
Folhas de Planta/efeitos da radiação
Folhas de Planta/ultraestrutura
Espécies Reativas de Oxigênio/metabolismo
Estresse Fisiológico
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Light-Harvesting Protein Complexes); 0 (Photosystem II Protein Complex); 0 (Reactive Oxygen Species); 0 (Thylakoid Membrane Proteins); 1406-65-1 (Chlorophyll); S88TT14065 (Oxygen)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160227
[St] Status:MEDLINE
[do] DOI:10.1111/ppl.12438



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