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Pesquisa : D12.776.157.530.450.162.276 [Categoria DeCS]
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  1 / 198 MEDLINE  
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[PMID]:27777302
[Au] Autor:Cheng B; Meng Y; Cui Y; Li C; Tao F; Yin H; Yang C; Xu P
[Ad] Endereço:From the State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100 and.
[Ti] Título:Alkaline Response of a Halotolerant Alkaliphilic Halomonas Strain and Functional Diversity of Its Na+(K+)/H+ Antiporters.
[So] Source:J Biol Chem;291(50):26056-26065, 2016 Dec 09.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Halomonas sp. Y2 is a halotolerant alkaliphilic strain from Na -rich pulp mill wastewater with high alkalinity (pH >11.0). Transcriptome analysis of this isolate revealed this strain may use various transport systems for pH homeostasis. In particular, the genes encoding four putative Na /H antiporters were differentially expressed upon acidic or alkaline conditions. Further evidence, from heterologous expression and mutant studies, suggested that Halomonas sp. Y2 employs its Na /H antiporters in a labor division way to deal with saline and alkaline environments. Ha-NhaD2 displayed robust Na (Li ) resistance and high transport activities in Escherichia coli; a ΔHa-nhaD2 mutant exhibited growth inhibition at high Na (Li ) concentrations at pH values of 6.2, 8.0, and 10.0, suggesting its physiological role in osmotic homeostasis. In contrast, Ha-NhaD1 showed much weaker activities in ion exporting and pH homeostasis. Ha-Mrp displayed a combination of properties similar to those of Mrp transporters from some Bacillus alkaliphiles and neutrophiles. This conferred obvious Na (Li , K ) resistance in E. coli-deficient strains, as those ion transport spectra of some neutrophil Mrp antiporters. Conversely, similar to the Bacillus alkaliphiles, Ha-Mrp showed central roles in the pH homeostasis of Halomonas sp. Y2. An Ha-mrp-disrupted mutant was seriously inhibited by high concentrations of Na (Li , K ) but only under alkaline conditions. Ha-NhaP was determined to be a K /H antiporter and shown to confer strong K resistance both at acidic and alkaline stresses.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Halomonas/metabolismo
Antiportadores de Potássio-Hidrogênio/metabolismo
Trocadores de Sódio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Halomonas/química
Halomonas/genética
Concentração de Íons de Hidrogênio
Mutação
Antiportadores de Potássio-Hidrogênio/química
Antiportadores de Potássio-Hidrogênio/genética
Trocadores de Sódio-Hidrogênio/química
Trocadores de Sódio-Hidrogênio/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Potassium-Hydrogen Antiporters); 0 (Sodium-Hydrogen Exchangers)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171209
[Lr] Data última revisão:
171209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  2 / 198 MEDLINE  
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[PMID]:28656748
[Au] Autor:Pliotas C; Grayer SC; Ekkerman S; Chan AKN; Healy J; Marius P; Bartlett W; Khan A; Cortopassi WA; Chandler SA; Rasmussen T; Benesch JLP; Paton RS; Claridge TDW; Miller S; Booth IR; Naismith JH; Conway SJ
[Ad] Endereço:Biomedical Sciences Research Complex, University of St Andrews , North Haugh, St Andrews KY16 9ST, U.K.
[Ti] Título:Adenosine Monophosphate Binding Stabilizes the KTN Domain of the Shewanella denitrificans Kef Potassium Efflux System.
[So] Source:Biochemistry;56(32):4219-4234, 2017 Aug 15.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ligand binding is one of the most fundamental properties of proteins. Ligand functions fall into three basic types: substrates, regulatory molecules, and cofactors essential to protein stability, reactivity, or enzyme-substrate complex formation. The regulation of potassium ion movement in bacteria is predominantly under the control of regulatory ligands that gate the relevant channels and transporters, which possess subunits or domains that contain Rossmann folds (RFs). Here we demonstrate that adenosine monophosphate (AMP) is bound to both RFs of the dimeric bacterial Kef potassium efflux system (Kef), where it plays a structural role. We conclude that AMP binds with high affinity, ensuring that the site is fully occupied at all times in the cell. Loss of the ability to bind AMP, we demonstrate, causes protein, and likely dimer, instability and consequent loss of function. Kef system function is regulated via the reversible binding of comparatively low-affinity glutathione-based ligands at the interface between the dimer subunits. We propose this interfacial binding site is itself stabilized, at least in part, by AMP binding.
[Mh] Termos MeSH primário: Monofosfato de Adenosina/química
Antiportadores de Potássio-Hidrogênio/química
Dobramento de Proteína
Multimerização Proteica
Shewanella/química
[Mh] Termos MeSH secundário: Monofosfato de Adenosina/genética
Monofosfato de Adenosina/metabolismo
Antiportadores de Potássio-Hidrogênio/genética
Antiportadores de Potássio-Hidrogênio/metabolismo
Ligação Proteica
Domínios Proteicos
Estabilidade Proteica
Estrutura Quaternária de Proteína
Shewanella/genética
Shewanella/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Potassium-Hydrogen Antiporters); 415SHH325A (Adenosine Monophosphate)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170629
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00300


  3 / 198 MEDLINE  
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[PMID]:27895227
[Au] Autor:Zhao S; Zhang ML; Ma TL; Wang Y
[Ad] Endereço:State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100193, China.
[Ti] Título:Phosphorylation of ARF2 Relieves Its Repression of Transcription of the K+ Transporter Gene HAK5 in Response to Low Potassium Stress.
[So] Source:Plant Cell;28(12):3005-3019, 2016 Dec.
[Is] ISSN:1532-298X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Potassium (K ) plays crucial roles in plant growth and development. In natural environments, K availability in soils is relatively low and fluctuating. Transcriptional regulation of K transporter genes is one of the most important mechanisms in the plant's response to K deficiency. In this study, we demonstrated that the transcription factor ARF2 (Auxin Response Factor 2) modulates the expression of the K transporter gene HAK5 (High Affinity K transporter 5) in Arabidopsis thaliana The arf2 mutant plants showed a tolerant phenotype similar to the HAK5-overexpressing lines on low-K medium, whose primary root lengths were longer than those of wild-type plants. High-affinity K uptake was significantly increased in these plants. ARF2-overexpressing lines and the hak5 mutant were both sensitive to low-K stress. Disruption of HAK5 in the arf2 mutant abolished the low-K -tolerant phenotype of arf2 As a transcriptional repressor, ARF2 directly bound to the HAK5 promoter and repressed HAK5 expression under K sufficient conditions. ARF2 can be phosphorylated after low-K treatment, which abolished its DNA binding activity to the HAK5 promoter and relieved the inhibition on HAK5 transcription. Therefore, HAK5 transcript could be induced, and HAK5-mediated high-affinity K uptake was enhanced under K deficient conditions. The presented results demonstrate that ARF2 plays important roles in the response to external K supply in Arabidopsis and regulates HAK5 transcription accordingly.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Antiportadores de Potássio-Hidrogênio/metabolismo
Potássio/metabolismo
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
Regulação da Expressão Gênica de Plantas/genética
Regulação da Expressão Gênica de Plantas/fisiologia
Fosforilação
Antiportadores de Potássio-Hidrogênio/genética
Proteínas Repressoras/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ARF2 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (Potassium-Hydrogen Antiporters); 0 (Repressor Proteins); 0 (potassium transporter, Arabidopsis); RWP5GA015D (Potassium)
[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:161130
[St] Status:MEDLINE
[do] DOI:10.1105/tpc.16.00684


  4 / 198 MEDLINE  
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[PMID]:27447945
[Au] Autor:Liu L; Zheng C; Kuang B; Wei L; Yan L; Wang T
[Ad] Endereço:Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing, China.
[Ti] Título:Receptor-Like Kinase RUPO Interacts with Potassium Transporters to Regulate Pollen Tube Growth and Integrity in Rice.
[So] Source:PLoS Genet;12(7):e1006085, 2016 07.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During sexual reproduction of flowering plants, the pollen tube grows fast and over a long distance within the pistil to deliver two sperms for double fertilization. Growing plant cells need to communicate constantly with external stimuli as well as monitor changes in surface tension of the cell wall and plasma membrane to coordinate these signals and internal growth machinery; however, the underlying mechanisms remain largely unknown. Here we show that the rice member of plant-specific receptor-like kinase CrRLK1Ls subfamily, Ruptured Pollen tube (RUPO), is specifically expressed in rice pollen. RUPO localizes to the apical plasma membrane and vesicle of pollen tubes and is required for male gamete transmission. K+ levels were greater in pollen of homozygous CRISPR-knockout lines than wild-type plants, and pollen tubes burst shortly after germination. We reveal the interaction of RUPO with high-affinity potassium transporters. Phosphorylation of RUPO established and dephosphorylation abolished the interaction. These results have revealed the receptor-like kinase as a regulator of high-affinity potassium transporters via phosphorylation-dependent interaction, and demonstrated a novel receptor-like kinase signaling pathway that mediates K+ homeostasis required for pollen tube growth and integrity.
[Mh] Termos MeSH primário: Proteínas de Membrana/genética
Oryza/genética
Proteínas de Plantas/genética
Tubo Polínico/genética
Antiportadores de Potássio-Hidrogênio/genética
Receptores Proteína Tirosina Quinases/genética
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
Flores/genética
Flores/crescimento & desenvolvimento
Regulação da Expressão Gênica de Plantas
Germinação/genética
Homeostase
Magnoliopsida/genética
Magnoliopsida/crescimento & desenvolvimento
Proteínas de Membrana/biossíntese
Oryza/crescimento & desenvolvimento
Fosforilação
Pólen/genética
Pólen/crescimento & desenvolvimento
Tubo Polínico/crescimento & desenvolvimento
Polinização/genética
Antiportadores de Potássio-Hidrogênio/biossíntese
Proteínas Quinases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Membrane Proteins); 0 (Plant Proteins); 0 (Potassium-Hydrogen Antiporters); EC 2.7.- (ANXUR1 protein, Arabidopsis); EC 2.7.- (ANXUR2 protein, Arabidopsis); EC 2.7.- (Protein Kinases); EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160723
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006085


  5 / 198 MEDLINE  
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[PMID]:27443603
[Au] Autor:Aranda-Sicilia MN; Aboukila A; Armbruster U; Cagnac O; Schumann T; Kunz HH; Jahns P; Rodríguez-Rosales MP; Sze H; Venema K
[Ad] Endereço:Departimento de Bioquímica, Biología Celular, y Molecular de Plantas, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, 18008 Granada, Spain (M.N.A.-S., A.A., O.C., M.P.R.-R., K.V.);Howard Hughes Medical Institute, Department of Plant and Microbial Biology, Universit
[Ti] Título:Envelope K+/H+ Antiporters AtKEA1 and AtKEA2 Function in Plastid Development.
[So] Source:Plant Physiol;172(1):441-9, 2016 Sep.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is well established that thylakoid membranes of chloroplasts convert light energy into chemical energy, yet the development of chloroplast and thylakoid membranes is poorly understood. Loss of function of the two envelope K(+)/H(+) antiporters AtKEA1 and AtKEA2 was shown previously to have negative effects on the efficiency of photosynthesis and plant growth; however, the molecular basis remained unclear. Here, we tested whether the previously described phenotypes of double mutant kea1kea2 plants are due in part to defects during early chloroplast development in Arabidopsis (Arabidopsis thaliana). We show that impaired growth and pigmentation is particularly evident in young expanding leaves of kea1kea2 mutants. In proliferating leaf zones, chloroplasts contain much lower amounts of photosynthetic complexes and chlorophyll. Strikingly, AtKEA1 and AtKEA2 proteins accumulate to high amounts in small and dividing plastids, where they are specifically localized to the two caps of the organelle separated by the fission plane. The unusually long amino-terminal domain of 550 residues that precedes the antiport domain appears to tether the full-length AtKEA2 protein to the two caps. Finally, we show that the double mutant contains 30% fewer chloroplasts per cell. Together, these results show that AtKEA1 and AtKEA2 transporters in specific microdomains of the inner envelope link local osmotic, ionic, and pH homeostasis to plastid division and thylakoid membrane formation.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Plastídeos/metabolismo
Antiportadores de Potássio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Arabidopsis/genética
Proteínas de Arabidopsis/classificação
Proteínas de Arabidopsis/genética
Clorofila/metabolismo
Cloroplastos/genética
Cloroplastos/metabolismo
Cloroplastos/ultraestrutura
Regulação da Expressão Gênica de Plantas
Homeostase
Concentração de Íons de Hidrogênio
Immunoblotting
Microscopia Confocal
Microscopia Eletrônica de Transmissão
Mutação
Osmose
Fotossíntese/genética
Complexo de Proteínas do Centro de Reação Fotossintética/genética
Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo
Filogenia
Folhas de Planta/genética
Folhas de Planta/metabolismo
Plantas Geneticamente Modificadas
Plastídeos/genética
Plastídeos/ultraestrutura
Antiportadores de Potássio-Hidrogênio/classificação
Antiportadores de Potássio-Hidrogênio/genética
Tilacoides/química
Tilacoides/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (KEA1 protein, Arabidopsis); 0 (Photosynthetic Reaction Center Complex Proteins); 0 (Potassium-Hydrogen Antiporters); 0 (potassium transporter, Arabidopsis); 1406-65-1 (Chlorophyll)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160723
[St] Status:MEDLINE
[do] DOI:10.1104/pp.16.00995


  6 / 198 MEDLINE  
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[PMID]:27335350
[Au] Autor:Armbruster U; Leonelli L; Correa Galvis V; Strand D; Quinn EH; Jonikas MC; Niyogi KK
[Ad] Endereço:Howard Hughes Medical Institute, Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA ute.armbruster78@gmail.com.
[Ti] Título:Regulation and Levels of the Thylakoid K+/H+ Antiporter KEA3 Shape the Dynamic Response of Photosynthesis in Fluctuating Light.
[So] Source:Plant Cell Physiol;57(7):1557-1567, 2016 Jul.
[Is] ISSN:1471-9053
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Crop canopies create environments of highly fluctuating light intensities. In such environments, photoprotective mechanisms and their relaxation kinetics have been hypothesized to limit photosynthetic efficiency and therefore crop yield potential. Here, we show that overexpression of the Arabidopsis thylakoid K /H antiporter KEA3 accelerates the relaxation of photoprotective energy-dependent quenching after transitions from high to low light in Arabidopsis and tobacco. This, in turn, enhances PSII quantum efficiency in both organisms, supporting that in wild-type plants, residual light energy quenching following a high to low light transition represents a limitation to photosynthetic efficiency in fluctuating light. This finding underscores the potential of accelerating quenching relaxation as a building block for improving photosynthetic efficiency in the field. Additionally, by overexpressing natural KEA3 variants with modification to the C-terminus, we show that KEA3 activity is regulated by a mechanism involving its lumen-localized C-terminus, which lowers KEA3 activity in high light. This regulatory mechanism fine-tunes the balance between photoprotective energy dissipation in high light and maximum quantum yield in low light, likely to be critical for efficient photosynthesis in fluctuating light conditions.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/fisiologia
Arabidopsis/efeitos da radiação
Luz
Fotossíntese/efeitos da radiação
Antiportadores de Potássio-Hidrogênio/metabolismo
Tilacoides/metabolismo
[Mh] Termos MeSH secundário: Processamento Alternativo/genética
Sequência de Aminoácidos
Arabidopsis/crescimento & desenvolvimento
Proteínas de Arabidopsis/química
Proteínas de Arabidopsis/genética
Sequência de Bases
Complexo de Proteína do Fotossistema II/metabolismo
Antiportadores de Potássio-Hidrogênio/química
Antiportadores de Potássio-Hidrogênio/genética
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Tilacoides/efeitos da radiação
Tabaco/fisiologia
Tabaco/efeitos da radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (KEA3 protein, Arabidopsis); 0 (Photosystem II Protein Complex); 0 (Potassium-Hydrogen Antiporters); 0 (Protein Isoforms); 0 (RNA, Messenger)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170327
[Lr] Data última revisão:
170327
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160624
[St] Status:MEDLINE


  7 / 198 MEDLINE  
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[PMID]:27208244
[Au] Autor:Brauer EK; Ahsan N; Dale R; Kato N; Coluccio AE; Piñeros MA; Kochian LV; Thelen JJ; Popescu SC
[Ad] Endereço:The Boyce Thompson Institute for Plant Research, Ithaca, New York 14853 (E.K.B., S.C.P.); Department of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, New York 14853 (E.K.B., S.C.P.); Department of Biochemistry, University of Missouri, Christopher S. Bond Life Sciences Center
[Ti] Título:The Raf-like Kinase ILK1 and the High Affinity K+ Transporter HAK5 Are Required for Innate Immunity and Abiotic Stress Response.
[So] Source:Plant Physiol;171(2):1470-84, 2016 Jun.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plant perception of pathogen-associated molecular patterns (PAMPs) and other environmental stresses trigger transient ion fluxes at the plasma membrane. Apart from the role of Ca(2+) uptake in signaling, the regulation and significance of PAMP-induced ion fluxes in immunity remain unknown. We characterized the functions of INTEGRIN-LINKED KINASE1 (ILK1) that encodes a Raf-like MAP2K kinase with functions insufficiently understood in plants. Analysis of ILK1 mutants impaired in the expression or kinase activity revealed that ILK1 contributes to plant defense to bacterial pathogens, osmotic stress sensitivity, and cellular responses and total ion accumulation in the plant upon treatment with a bacterial-derived PAMP, flg22. The calmodulin-like protein CML9, a negative modulator of flg22-triggered immunity, interacted with, and suppressed ILK1 kinase activity. ILK1 interacted with and promoted the accumulation of HAK5, a putative (H(+))/K(+) symporter that mediates a high-affinity uptake during K(+) deficiency. ILK1 or HAK5 expression was required for several flg22 responses including gene induction, growth arrest, and plasma membrane depolarization. Furthermore, flg22 treatment induced a rapid K(+) efflux at both the plant and cellular levels in wild type, while mutants with impaired ILK1 or HAK5 expression exhibited a comparatively increased K(+) loss. Taken together, our results position ILK1 as a link between plant defense pathways and K(+) homeostasis.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/imunologia
Arabidopsis/fisiologia
Imunidade Inata
Imunidade Vegetal
Antiportadores de Potássio-Hidrogênio/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Estresse Fisiológico
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Arabidopsis/genética
Arabidopsis/microbiologia
Calmodulina/metabolismo
Flagelina/farmacologia
Homeostase/efeitos dos fármacos
Imunidade Inata/efeitos dos fármacos
Íons
Manitol/farmacologia
Modelos Biológicos
Mutação/genética
Osmose/efeitos dos fármacos
Doenças das Plantas/imunologia
Doenças das Plantas/microbiologia
Imunidade Vegetal/efeitos dos fármacos
Plantas Geneticamente Modificadas
Potássio/metabolismo
Ligação Proteica/efeitos dos fármacos
Transporte Proteico/efeitos dos fármacos
Proteínas Serina-Treonina Quinases/química
Transdução de Sinais/efeitos dos fármacos
Cloreto de Sódio/farmacologia
Estresse Fisiológico/efeitos dos fármacos
Frações Subcelulares/efeitos dos fármacos
Frações Subcelulares/metabolismo
Tabaco/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (CaM9 protein, Arabidopsis); 0 (Calmodulin); 0 (Ions); 0 (Potassium-Hydrogen Antiporters); 0 (potassium transporter, Arabidopsis); 12777-81-0 (Flagellin); 3OWL53L36A (Mannitol); 451W47IQ8X (Sodium Chloride); EC 2.7.1.- (ILK1 protein, Arabidopsis); EC 2.7.1.- (integrin-linked kinase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); RWP5GA015D (Potassium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160522
[St] Status:MEDLINE
[do] DOI:10.1104/pp.16.00035


  8 / 198 MEDLINE  
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[PMID]:27203707
[Au] Autor:Ariyarathna HA; Francki MG
[Ad] Endereço:a School of Plant Biology and Institute of Agriculture, The University of Western Australia, Crawley WA 6009, Australia.
[Ti] Título:Phylogenetic relationships and protein modelling revealed two distinct subfamilies of group II HKT genes between crop and model grasses.
[So] Source:Genome;59(7):509-17, 2016 Jul.
[Is] ISSN:1480-3321
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:Molecular evolution of large protein families in closely related species can provide useful insights on structural functional relationships. Phylogenetic analysis of the grass-specific group II HKT genes identified two distinct subfamilies, I and II. Subfamily II was represented in all species, whereas subfamily I was identified only in the small grain cereals and possibly originated from an ancestral gene duplication post divergence from the coarse grain cereal lineage. The core protein structures were highly analogous despite there being no more than 58% amino acid identity between members of the two subfamilies. Distinctly variable regions in known functional domains, however, indicated functional divergence of the two subfamilies. The subsets of codons residing external to known functional domains predicted signatures of positive Darwinian selection potentially identifying new domains of functional divergence and providing new insights on the structural function and relationships between protein members of the two subfamilies.
[Mh] Termos MeSH primário: Família Multigênica/genética
Poaceae/genética
Antiportadores de Potássio-Hidrogênio/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência de Bases
Códon
Produtos Agrícolas/genética
Produtos Agrícolas/metabolismo
DNA Complementar/genética
Evolução Molecular
Duplicação Gênica
Genes de Plantas
Oryza/genética
Oryza/metabolismo
Filogenia
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Poaceae/metabolismo
Antiportadores de Potássio-Hidrogênio/metabolismo
Estrutura Terciária de Proteína
Seleção Genética
Alinhamento de Sequência
Triticum/genética
Triticum/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon); 0 (DNA, Complementary); 0 (Plant Proteins); 0 (Potassium-Hydrogen Antiporters)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170404
[Lr] Data última revisão:
170404
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160521
[St] Status:MEDLINE
[do] DOI:10.1139/gen-2016-0035


  9 / 198 MEDLINE  
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[PMID]:27080934
[Au] Autor:Dana S; Herdean A; Lundin B; Spetea C
[Ad] Endereço:Department of Biological and Environmental Sciences, University of Gothenburg, Gothenburg 40530, Sweden.
[Ti] Título:Each of the chloroplast potassium efflux antiporters affects photosynthesis and growth of fully developed Arabidopsis rosettes under short-day photoperiod.
[So] Source:Physiol Plant;158(4):483-491, 2016 Dec.
[Is] ISSN:1399-3054
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:In Arabidopsis thaliana, the chloroplast harbors three potassium efflux antiporters (KEAs), namely KEA1 and KEA2 in the inner envelope and KEA3 in the thylakoid membrane. They may play redundant physiological roles as in our previous analyses of young developing Arabidopsis rosettes under long-day photoperiod (16 h light per day), chloroplast kea single mutants resembled the wild-type plants, whereas kea1kea2 and kea1kea2kea3 mutants were impaired in chloroplast development and photosynthesis resulting in stunted growth. Here, we aimed to study whether chloroplast KEAs play redundant roles in chloroplast function of older Arabidopsis plants with fully developed rosettes grown under short-day photoperiod (8 h light per day). Under these conditions, we found defects in photosynthesis and growth in the chloroplast kea single mutants, and most dramatic defects in the kea1kea2 double mutant. The mechanism behind these defects in the single mutants involves reduction in the electron transport rate (kea1 and kea3), and stomata conductance (kea1, kea2 and kea3), which in turn affect CO fixation rates. The kea1kea2 mutant, in addition to these alterations, displayed reduced levels of photosynthetic machinery. Taken together, our data suggest that, in addition to the previously reported roles in chloroplast development in young rosettes, each chloroplast KEA affects photosynthesis and growth of Arabidopsis fully developed rosettes.
[Mh] Termos MeSH primário: Arabidopsis/crescimento & desenvolvimento
Cloroplastos/fisiologia
Fotossíntese/fisiologia
Antiportadores de Potássio-Hidrogênio/fisiologia
[Mh] Termos MeSH secundário: Arabidopsis/metabolismo
Arabidopsis/fisiologia
Carotenoides/análise
Carotenoides/fisiologia
Clorofila/análise
Clorofila/fisiologia
Cloroplastos/metabolismo
Mutação
Fotoperíodo
Folhas de Planta/química
Folhas de Planta/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Potassium-Hydrogen Antiporters); 1406-65-1 (Chlorophyll); 36-88-4 (Carotenoids)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170421
[Lr] Data última revisão:
170421
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160416
[St] Status:MEDLINE
[do] DOI:10.1111/ppl.12452


  10 / 198 MEDLINE  
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[PMID]:26966178
[Au] Autor:Wu X; Kim H; Seravalli J; Barycki JJ; Hart PJ; Gohara DW; Di Cera E; Jung WH; Kosman DJ; Lee J
[Ad] Endereço:From the Department of Biochemistry and Redox Biology Center, University of Nebraska-Lincoln, Lincoln, Nebraska 68588-0664, College of Life and Environmental Sciences, Shanghai Normal University, Shanghai, China 200234.
[Ti] Título:Potassium and the K+/H+ Exchanger Kha1p Promote Binding of Copper to ApoFet3p Multi-copper Ferroxidase.
[So] Source:J Biol Chem;291(18):9796-806, 2016 Apr 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acquisition and distribution of metal ions support a number of biological processes. Here we show that respiratory growth of and iron acquisition by the yeast Saccharomyces cerevisiae relies on potassium (K(+)) compartmentalization to the trans-Golgi network via Kha1p, a K(+)/H(+) exchanger. K(+) in the trans-Golgi network facilitates binding of copper to the Fet3p multi-copper ferroxidase. The effect of K(+) is not dependent on stable binding with Fet3p or alteration of the characteristics of the secretory pathway. The data suggest that K(+) acts as a chemical factor in Fet3p maturation, a role similar to that of cations in folding of nucleic acids. Up-regulation of KHA1 gene in response to iron limitation via iron-specific transcription factors indicates that K(+) compartmentalization is linked to cellular iron homeostasis. Our study reveals a novel functional role of K(+) in the binding of copper to apoFet3p and identifies a K(+)/H(+) exchanger at the secretory pathway as a new molecular factor associated with iron uptake in yeast.
[Mh] Termos MeSH primário: Ceruloplasmina/metabolismo
Cobre/metabolismo
Regulação Fúngica da Expressão Gênica/fisiologia
Antiportadores de Potássio-Hidrogênio/biossíntese
Proteínas de Saccharomyces cerevisiae/biossíntese
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Regulação para Cima/fisiologia
[Mh] Termos MeSH secundário: Ceruloplasmina/genética
Ferro
Potássio/metabolismo
Antiportadores de Potássio-Hidrogênio/genética
Ligação Proteica
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (KHA1 protein, S cerevisiae); 0 (Potassium-Hydrogen Antiporters); 0 (Saccharomyces cerevisiae Proteins); 789U1901C5 (Copper); E1UOL152H7 (Iron); EC 1.16.3.1 (Ceruloplasmin); EC 1.16.3.1 (FET3 protein, S cerevisiae); RWP5GA015D (Potassium)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170429
[Lr] Data última revisão:
170429
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160312
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.700500



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