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  1 / 162 MEDLINE  
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PMID:27278067
Autor:Sun J; Hu H; Li Y; Wang L; Zhou Q; Huang X
Endereço:State Key Laboratory of Food Science and Technology, Jiangsu Key Laboratory of Anaerobic Biotechnology, College of Environment and Civil Engineering, Jiangnan University, Wuxi, 214122, China.
Título:Effects and mechanism of acid rain on plant chloroplast ATP synthase.
Fonte:Environ Sci Pollut Res Int; 23(18):18296-306, 2016 Sep.
ISSN:1614-7499
País de publicação:Germany
Idioma:eng
Resumo:Acid rain can directly or indirectly affect plant physiological functions, especially photosynthesis. The enzyme ATP synthase is the key in photosynthetic energy conversion, and thus, it affects plant photosynthesis. To clarify the mechanism by which acid rain affects photosynthesis, we studied the effects of acid rain on plant growth, photosynthesis, chloroplast ATP synthase activity and gene expression, chloroplast ultrastructure, intracellular H(+) level, and water content of rice seedlings. Acid rain at pH 4.5 remained the chloroplast structure unchanged but increased the expression of six chloroplast ATP synthase subunits, promoted chloroplast ATP synthase activity, and increased photosynthesis and plant growth. Acid rain at pH 4.0 or less decreased leaf water content, destroyed chloroplast structure, inhibited the expression of six chloroplast ATP synthase subunits, decreased chloroplast ATP synthase activity, and reduced photosynthesis and plant growth. In conclusion, acid rain affected the chloroplast ultrastructure, chloroplast ATPase transcription and activity, and P n by changing the acidity in the cells, and thus influencing the plant growth and development. Finally, the effects of simulated acid rain on the test indices were found to be dose-dependent.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Acid Rain); EC 3.6.3.- (Chloroplast Proton-Translocating ATPases)


  2 / 162 MEDLINE  
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PMID:27233821
Autor:Carrillo LR; Froehlich JE; Cruz JA; Savage LJ; Kramer DM
Endereço:Biochemistry & Molecular Biology, Michigan State University, 612 Wilson Road, Rm 106, East Lansing, MI, 48824, USA.
Título:Multi-level regulation of the chloroplast ATP synthase: the chloroplast NADPH thioredoxin reductase C (NTRC) is required for redox modulation specifically under low irradiance.
Fonte:Plant J; 87(6):654-63, 2016 Sep.
ISSN:1365-313X
País de publicação:England
Idioma:eng
Resumo:The chloroplast ATP synthase is known to be regulated by redox modulation of a disulfide bridge on the γ-subunit through the ferredoxin-thioredoxin regulatory system. We show that a second enzyme, the recently identified chloroplast NADPH thioredoxin reductase C (NTRC), plays a role specifically at low irradiance. Arabidopsis mutants lacking NTRC (ntrc) displayed a striking photosynthetic phenotype in which feedback regulation of the light reactions was strongly activated at low light, but returned to wild-type levels as irradiance was increased. This effect was caused by an altered redox state of the γ-subunit under low, but not high, light. The low light-specific decrease in ATP synthase activity in ntrc resulted in a buildup of the thylakoid proton motive force with subsequent activation of non-photochemical quenching and downregulation of linear electron flow. We conclude that NTRC provides redox modulation at low light using the relatively oxidizing substrate NADPH, whereas the canonical ferredoxin-thioredoxin system can take over at higher light, when reduced ferredoxin can accumulate. Based on these results, we reassess previous models for ATP synthase regulation and propose that NTRC is most likely regulated by light. We also find that ntrc is highly sensitive to rapidly changing light intensities that probably do not involve the chloroplast ATP synthase, implicating this system in multiple photosynthetic processes, particularly under fluctuating environmental conditions.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Arabidopsis Proteins); EC 1.8.1.9 (NTRC protein, Arabidopsis); EC 1.8.1.9 (Thioredoxin-Disulfide Reductase); EC 3.6.3.- (Chloroplast Proton-Translocating ATPases)


  3 / 162 MEDLINE  
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PMID:27208269
Autor:Zhang L; Duan Z; Zhang J; Peng L
Endereço:Key Laboratory of Photobiology, CAS Center for Excellence in Molecular Plant Sciences, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China (L.Z., Z.D., J.Z., L.P.); andUniversity of Chinese Academy of Sciences, Beijing 100049, China (L.Z., Z.D.).
Título:BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex.
Fonte:Plant Physiol; 171(2):1291-306, 2016 Jun.
ISSN:1532-2548
País de publicação:United States
Idioma:eng
Resumo:Thylakoid membrane-localized chloroplast ATP synthases use the proton motive force generated by photosynthetic electron transport to produce ATP from ADP. Although it is well known that the chloroplast ATP synthase is composed of more than 20 proteins with α3ß3γ1ε1δ1I1II1III14IV1 stoichiometry, its biogenesis process is currently unclear. To unravel the molecular mechanisms underlying the biogenesis of chloroplast ATP synthase, we performed extensive screening for isolating ATP synthase mutants in Arabidopsis (Arabidopsis thaliana). In the recently identified bfa3 (biogenesis factors required for ATP synthase 3) mutant, the levels of chloroplast ATP synthase subunits were reduced to approximately 25% of wild-type levels. In vivo labeling analysis showed that assembly of the CF1 component of chloroplast ATP synthase was less efficient in bfa3 than in the wild type, indicating that BFA3 is required for CF1 assembly. BFA3 encodes a chloroplast stromal protein that is conserved in higher plants, green algae, and a few species of other eukaryotic algae, and specifically interacts with the CF1ß subunit. The BFA3 binding site was mapped to a region in the catalytic site of CF1ß. Several residues highly conserved in eukaryotic CF1ß are crucial for the BFA3-CF1ß interaction, suggesting a coevolutionary relationship between BFA3 and CF1ß. BFA3 appears to function as a molecular chaperone that transiently associates with unassembled CF1ß at its catalytic site and facilitates subsequent association with CF1α during assembly of the CF1 subcomplex of chloroplast ATP synthase.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Arabidopsis Proteins); 0 (Membrane Proteins); 0 (Protein Subunits); 0 (biogenesis factor required for ATP synthase 3, Arabidopsis); EC 3.6.3.- (Chloroplast Proton-Translocating ATPases)


  4 / 162 MEDLINE  
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PMID:26979383
Autor:Grahl S; Reiter B; Gügel IL; Vamvaka E; Gandini C; Jahns P; Soll J; Leister D; Rühle T
Endereço:Lehrstuhl für Biochemie und Physiologie der Pflanzen (Botanik), Department Biologie I, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany; Munich Centre for Integrated Protein Science CiPSM, Ludwig-Maximilians Universität München, Butenandtstr. 5 - 13, 81377 Munich, Germany.
Título:The Arabidopsis Protein CGLD11 Is Required for Chloroplast ATP Synthase Accumulation.
Fonte:Mol Plant; 9(6):885-99, 2016 06 06.
ISSN:1752-9867
País de publicação:England
Idioma:eng
Resumo:ATP synthases in chloroplasts (cpATPase) and mitochondria (mtATPase) are responsible for ATP production during photosynthesis and oxidative phosphorylation, respectively. Both enzymes consist of two multisubunit complexes, the membrane-bound coupling factor O and the soluble coupling factor 1. During cpATPase biosynthesis, several accessory factors facilitate subunit production and orchestrate complex assembly. Here, we describe a new auxiliary protein in Arabidopsis thaliana, which is required for cpATPase accumulation. AtCGLD11 (CONSERVED IN THE GREEN LINEAGE AND DIATOMS 11) is a protein without any known functional domain and shows dual localization to chloroplasts and mitochondria. Loss of AtCGLD11 function results in reduced levels of cpATPase and impaired photosynthetic performance with lower rates of ATP synthesis. In yeast two-hybrid experiments, AtCGLD11 interacts with the ß subunits of the cpATPase and mtATPase. Our results suggest that AtCGLD11 functions in F1 assembly during cpATPase biogenesis, while its role in mtATPase biosynthesis may not, or not yet, be essential.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Arabidopsis Proteins); EC 3.6.3.- (Chloroplast Proton-Translocating ATPases)


  5 / 162 MEDLINE  
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PMID:26754050
Autor:Malyan AN
Endereço:Institute of Basic Biological Problems Russian Academy of Sciences, Pushchino, Russia. alexander.malyan@gmail.com.
Título:The effect of medium viscosity on kinetics of ATP hydrolysis by the chloroplast coupling factor CF1.
Fonte:Photosynth Res; 128(2):163-8, 2016 May.
ISSN:1573-5079
País de publicação:Netherlands
Idioma:eng
Resumo:The coupling factor CF1 is a catalytic part of chloroplast ATP synthase which is exposed to stroma whose viscosity is many-fold higher than that of reaction mixtures commonly used to measure kinetics of CF1-catalyzed ATP hydrolysis. This study is focused on the effect of medium viscosity modulated by sucrose or bovine serum albumin (BSA) on kinetics of Ca(2+)- and Mg(2+)-dependent ATP hydrolysis by CF1. These agents were shown to reduce the maximal rate of Ca(2+)-dependent ATPase without changing the apparent Michaelis constant (К m), thus supporting the hypothesis on viscosity dependence of CF1 activity. For the sulfite- and ethanol-stimulated Mg(2+)-dependent reaction, the presence of sucrose increased К m without changing the maximal rate that is many-fold as high as that of Ca(2+)-dependent hydrolysis. The hydrolysis reaction was shown to be stimulated by low concentrations of BSA and inhibited by its higher concentrations, with the increasing maximal reaction rate estimated by extrapolation. Sucrose- or BSA-induced inhibition of the Mg(2+)-dependent ATPase reaction is believed to result from diffusion-caused deceleration, while its BSA-induced stimulation is probably caused by optimization of the enzyme structure. Molecular mechanisms of the inhibitory effect of viscosity are discussed. Taking into account high protein concentrations in the chloroplast stroma, it was suggested that kinetic parameters of ATP hydrolysis, and probably those of ATP synthesis in vivo as well, must be quite different from measurements taken at a viscosity level close to that of water.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Culture Media); 27432CM55Q (Serum Albumin, Bovine); 57-50-1 (Sucrose); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.3.- (Chloroplast Proton-Translocating ATPases); I38ZP9992A (Magnesium); SY7Q814VUP (Calcium)


  6 / 162 MEDLINE  
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PMID:26669008
Autor:Guo DD; Guo QH; Gao Y; Guo ML
Título:Expression of ATP synthase CF1 alpha subunit gene (CTL-spn) as screened by the cDNA-SRAP approach is correlated with spininess in Carthamus tinctorius L.
Fonte:Yao Xue Xue Bao; 50(8):1052-9, 2015 Aug.
ISSN:0513-4870
País de publicação:China
Idioma:eng
Resumo:The safflower floret is a traditional Chinese medicine used to promote blood circulation and remove obstruction in the channels. The spines on its bracts are considered a handicap when manual harvest is involved. In this study, cDNA-SRAP was used to systematically investigate which genes are associated with the spines. Sixty pairs of possible primer combinations were used on two cDNA pools representing spininess and spinelessness. Six transcript-derived fragments were identified, of which two with low recombination were sequenced successfully and named as GPY-1 and GPY-2. By using the RACE method, the full-length cDNA of GPY-2 is cloned and named as CTL-spn. The full-length cDNA of CTL-spn was 1 679 bp long with a 1 524 bp ORF encoding a 508 aminoacid protein. The deduced amino acid sequence of the CTL-spn gene shared a high homology (97%) with other known ATP synthase CF1 alpha subunits. Semiquantitative RT-PCR analysis revealed that the mRNA of GPY-1 and GPY-2 accumulated in only spiny lines. Considering the important role of ATP synthase CF1 alpha subunit in plants, it may directly take part in the formation process of spininess and enhancing resistance reaction of spiny safflower. Also, our results provide the important insights for breeding spineless cultivars of safflower.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (DNA Primers); 0 (DNA, Complementary); 0 (Plant Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.3.- (Chloroplast Proton-Translocating ATPases)


  7 / 162 MEDLINE  
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PMID:26499367
Autor:Tu Y; Jin Y; Ma D; Li H; Zhang Z; Dong J; Wang T
Endereço:State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing 100193, China.
Título:Interaction between PVY HC-Pro and the NtCF1ß-subunit reduces the amount of chloroplast ATP synthase in virus-infected tobacco.
Fonte:Sci Rep; 5:15605, 2015 Oct 26.
ISSN:2045-2322
País de publicação:England
Idioma:eng
Resumo:The photosynthetic rate of virus-infected plants is always reduced. However, the molecular mechanism underlying this phenomenon remains unclear. The helper component-proteinase (HC-Pro) of Potato virus Y (PVY) was found in the chloroplasts of PVY-infected tobacco, indicating some new function of HC-Pro in the chloroplasts. We generated HC-Pro transgenic plants with a transit peptide to target the protein to chloroplast. The HC-Pro transgenic tobacco showed a decreased photosynthetic rate by 25% at the light intensity of 600 µmol m(-2) s(-1). Using a yeast two-hybrid screening assay to search for chloroplast proteins interacting with HC-Pro, we identified that PVY HC-Pro can interact with the chloroplast ATP synthase NtCF1ß-subunit. This interaction was confirmed by GST pull-down and co-immunoprecipitation assays. HC-Pro didn't interfere with the activity of assembled ATP synthase in vitro. The HC-Pro/NtCF1ß-subunit interaction might affect the assembly of ATP synthase complex. Quantitative western blot and immunogold labeling of the ATP synthase indicated that the amount of ATP synthase complex was decreased in both the HC-Pro transgenic and the PVY-infected tobacco. These results demonstrate that HC-Pro plays an important role in reducing the photosynthetic rate of PVY-infected plants, which is a completely new role of HC-Pro besides its multiple known functions.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Viral Proteins); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.- (HC-Pro protein, potyvirus); EC 3.6.3.- (Chloroplast Proton-Translocating ATPases)


  8 / 162 MEDLINE  
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PMID:26349211
Autor:Kartashov IM; Opanasenko VK; Malyan AN
Título:[Effects of Medium Viscosity Increasing Agents on ATP Synthesis in Chloroplast Thylakoids].
Fonte:Biofizika; 60(3):481-6, 2015 May-Jun.
ISSN:0006-3029
País de publicação:Russia (Federation)
Idioma:rus
Resumo:The effect of an increase in the medium viscosity on cyclic photophosphorylation in chloroplast thylakoids and on Ca2+ -dependent ATP hydrolysis by the chloroplast coupling factor CF, was studied. With 0.1-0.2 mM ADP used it was found that the rate of ATP synthesis decreases after addition of various agents that increase the medium viscosity (sucrose, dextran 40 or polyethylene glycol 6000 provided that these agents cause neither uncoupling nor electron transport inhibition in the absence of ADP. Dextran and polyethylene glycol inhibited ATP synthesis by 50% when their concentrations were much lower (6-10%) than that of sucrose (30-40%), while 50% inhibition of Ca2+ -dependent ATP hydrolysis by CFI-ATPase was observed at higher concentrations of dextran and polyethylene glycol (9-13%) and lower concentrations of sucrose (about 20%). For ADP, the effective Michaelis constant (KM) was shown to increase 2-3-fold with the increasing viscosity; meanwhile the maximal rate of cyclic photophosphorylation remained virtually unchanged. The dependence of K(M) on the medium viscosity can serve as a criterion for the process of diffusion-controlled photophosphorylation. Possible mechanisms of ADP and ATP diffusion are discussed.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Culture Media); 0 (Dextrans); 30IQX730WE (Polyethylene Glycols); 57-50-1 (Sucrose); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.3.- (Chloroplast Proton-Translocating ATPases); SY7Q814VUP (Calcium)


  9 / 162 MEDLINE  
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PMID:26182363
Autor:Sautron E; Mayerhofer H; Giustini C; Pro D; Crouzy S; Ravaud S; Pebay-Peyroula E; Rolland N; Catty P; Seigneurin-Berny D
Endereço:CNRS, Laboratoire de Physiologie Cellulaire et Végétale, UMR 5168, 17 rue des Martyrs, F-38054 Grenoble, France Univ. Grenoble Alpes, F-38054 Grenoble, France CEA, DSV, iRTSV, F-38054 Grenoble, France INRA, LPCV, USC1359, 17 rue des Martyrs, F-38054 Grenoble, France.
Título:HMA6 and HMA8 are two chloroplast Cu+-ATPases with different enzymatic properties.
Fonte:Biosci Rep; 35(3), 2015 Apr 20.
ISSN:1573-4935
País de publicação:England
Idioma:eng
Resumo:Copper (Cu) plays a key role in the photosynthetic process as cofactor of the plastocyanin (PC), an essential component of the chloroplast photosynthetic electron transfer chain. Encoded by the nuclear genome, PC is translocated in its apo-form into the chloroplast and the lumen of thylakoids where it is processed to its mature form and acquires Cu. In Arabidopsis, Cu delivery into the thylakoids involves two transporters of the PIB-1 ATPases family, heavy metal associated protein 6 (HMA6) located at the chloroplast envelope and HMA8 at the thylakoid membrane. To gain further insight into the way Cu is delivered to PC, we analysed the enzymatic properties of HMA8 and compared them with HMA6 ones using in vitro phosphorylation assays and phenotypic tests in yeast. These experiments reveal that HMA6 and HMA8 display different enzymatic properties: HMA8 has a higher apparent affinity for Cu(+) but a slower dephosphorylation kinetics than HMA6. Modelling experiments suggest that these differences could be explained by the electrostatic properties of the Cu(+) releasing cavities of the two transporters and/or by the different nature of their cognate Cu(+) acceptors (metallochaperone/PC).
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Arabidopsis Proteins); 0 (HMA8 protein, Arabidopsis); 789U1901C5 (Copper); 8L70Q75FXE (Adenosine Triphosphate); 9014-09-9 (Plastocyanin); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (HMA6 protein, Arabidopsis); EC 3.6.3.- (Chloroplast Proton-Translocating ATPases)


  10 / 162 MEDLINE  
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PMID:26055710
Autor:Bell AJ; Frankel LK; Bricker TM
Endereço:From the Department of Biological Sciences, Biochemistry and Molecular Biology Section, Louisiana State University, Baton Rouge, Louisiana 70803.
Título:High Yield Non-detergent Isolation of Photosystem I-Light-harvesting Chlorophyll II Membranes from Spinach Thylakoids: IMPLICATIONS FOR THE ORGANIZATION OF THE PS I ANTENNAE IN HIGHER PLANTS.
Fonte:J Biol Chem; 290(30):18429-37, 2015 Jul 24.
ISSN:1083-351X
País de publicação:United States
Idioma:eng
Resumo:Styrene-maleic acid copolymer was used to effect a non-detergent partial solubilization of thylakoids from spinach. A high density membrane fraction, which was not solubilized by the copolymer, was isolated and was highly enriched in the Photosystem (PS) I-light-harvesting chlorophyll (LHC) II supercomplex and depleted of PS II, the cytochrome b6/f complex, and ATP synthase. The LHC II associated with the supercomplex appeared to be energetically coupled to PS I based on 77 K fluorescence, P700 photooxidation, and PS I electron transport light saturation experiments. The chlorophyll (Chl) a/b ratio of the PS I-LHC II membranes was 3.2 ± 0.9, indicating that on average, three LHC II trimers may associate with each PS I. The implication of these findings within the context of higher plant PS I antenna organization is discussed.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
Nome de substância:0 (Light-Harvesting Protein Complexes); 0 (Maleic Anhydrides); 0 (Photosystem I Protein Complex); 0 (Photosystem II Protein Complex); 0 (Polystyrenes); 9011-13-6 (Styromal); 9035-40-9 (Cytochrome b6f Complex); EC 3.6.3.- (Chloroplast Proton-Translocating ATPases)



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