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[PMID]:28861701
[Au] Autor:Savada RP; Ozga JA; Jayasinghege CPA; Waduthanthri KD; Reinecke DM
[Ad] Endereço:Plant BioSystems Division, Department of Agricultural, Food and Nutritional Science, 4-10 Agriculture/Forestry Centre, University of Alberta, Edmonton, AB, T6G 2P5, Canada.
[Ti] Título:Heat stress differentially modifies ethylene biosynthesis and signaling in pea floral and fruit tissues.
[So] Source:Plant Mol Biol;95(3):313-331, 2017 Oct.
[Is] ISSN:1573-5028
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: Ethylene biosynthesis is regulated in reproductive tissues in response to heat stress in a manner to optimize resource allocation to pollinated fruits with developing seeds. High temperatures during reproductive development are particularly detrimental to crop fruit/seed production. Ethylene plays vital roles in plant development and abiotic stress responses; however, little is known about ethylene's role in reproductive tissues during development under heat stress. We assessed ethylene biosynthesis and signaling regulation within the reproductive and associated tissues of pea during the developmental phase that sets the stage for fruit-set and seed development under normal and heat-stress conditions. The transcript abundance profiles of PsACS [encode enzymes that convert S-adenosyl-L-methionine to 1-aminocyclopropane-1-carboxylic acid (ACC)] and PsACO (encode enzymes that convert ACC to ethylene), and ethylene evolution were developmentally, environmentally, and tissue-specifically regulated in the floral/fruit/pedicel tissues of pea. Higher transcript abundance of PsACS and PsACO in the ovaries, and PsACO in the pedicels was correlated with higher ethylene evolution and ovary senescence and pedicel abscission in fruits that were not pollinated under control temperature conditions. Under heat-stress conditions, up-regulation of ethylene biosynthesis gene expression in pre-pollinated ovaries was also associated with higher ethylene evolution and lower retention of these fruits. Following successful pollination and ovule fertilization, heat-stress modified PsACS and PsACO transcript profiles in a manner that suppressed ovary ethylene evolution. The normal ethylene burst in the stigma/style and petals following pollination was also suppressed by heat-stress. Transcript abundance profiles of ethylene receptor and signaling-related genes acted as qualitative markers of tissue ethylene signaling events. These data support the hypothesis that ethylene biosynthesis is regulated in reproductive tissues in response to heat stress to modulate resource allocation dynamics.
[Mh] Termos MeSH primário: Etilenos/biossíntese
Flores/metabolismo
Frutas/metabolismo
Temperatura Alta
Ervilhas/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Aminoácidos Cíclicos/metabolismo
Flores/genética
Flores/crescimento & desenvolvimento
Frutas/genética
Frutas/crescimento & desenvolvimento
Regulação da Expressão Gênica no Desenvolvimento
Regulação da Expressão Gênica de Plantas
Liases/genética
Liases/metabolismo
Ervilhas/genética
Ervilhas/crescimento & desenvolvimento
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Polinização/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Sementes/genética
Sementes/crescimento & desenvolvimento
Sementes/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Cyclic); 0 (Ethylenes); 0 (Plant Proteins); 3K9EJ633GL (1-aminocyclopropane-1-carboxylic acid); EC 4.- (Lyases); EC 4.4.1.14 (1-aminocyclopropanecarboxylate synthase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170902
[St] Status:MEDLINE
[do] DOI:10.1007/s11103-017-0653-1


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[PMID]:28683918
[Au] Autor:Dey M
[Ad] Endereço:The University of Iowa, Iowa City, IA, United States. Electronic address: mishtu-dey@uiowa.edu.
[Ti] Título:Enzymology of Microbial Dimethylsulfoniopropionate Catabolism.
[So] Source:Adv Protein Chem Struct Biol;109:195-222, 2017.
[Is] ISSN:1876-1623
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The biochemistry of dimethylsulfoniopropionate (DMSP) catabolism is reviewed. The microbes that catalyze the reactions central to DMSP catabolic pathways are described, and the focus is on the enzymology of the process. Approximately 10 tons of DMSP is released annually by marine eukaryotes as an osmolyte. A vast majority of DMSP is assimilated by bacteria through either a demethylation or lyase pathways, producing either the methane thiol or the volatile dimethylsulfide (DMS), respectively. Enzymatic breakdown of DMSP generates ~10 tons of DMS annually, which may have impact on global climate. DMS also acts as a chemoattractant for zooplanktons and seabirds. Both DMSP and DMS play a key role in the global sulfur cycle and are key nutrients for marine microbial growth. Important enzymes in the biochemical pathways of DMSP catabolism are covered in this review, with a focus on the latest developments in their mechanism.
[Mh] Termos MeSH primário: Bactérias/enzimologia
Bactérias/metabolismo
Proteínas de Bactérias/metabolismo
Compostos de Sulfônio/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bactérias/química
Bactérias/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Coenzima A-Transferases/química
Coenzima A-Transferases/genética
Coenzima A-Transferases/metabolismo
Regulação Bacteriana da Expressão Gênica
Liases/química
Liases/genética
Liases/metabolismo
Redes e Vias Metabólicas
Modelos Moleculares
Conformação Proteica
Proteobactérias/química
Proteobactérias/enzimologia
Proteobactérias/genética
Proteobactérias/metabolismo
Compostos de Sulfônio/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Sulfonium Compounds); C884XA7QGG (dimethylpropiothetin); EC 2.8.3.- (Coenzyme A-Transferases); EC 4.- (Lyases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE


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[PMID]:28629946
[Au] Autor:Mezzar S; De Schryver E; Asselberghs S; Meyhi E; Morvay PL; Baes M; Van Veldhoven PP
[Ad] Endereço:LIPIT, Department of Cellular and Molecular Medicine, KU Leuven, Belgium.
[Ti] Título:Phytol-induced pathology in 2-hydroxyacyl-CoA lyase (HACL1) deficient mice. Evidence for a second non-HACL1-related lyase.
[So] Source:Biochim Biophys Acta;1862(9):972-990, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:2-Hydroxyacyl-CoA lyase (HACL1) is a key enzyme of the peroxisomal α-oxidation of phytanic acid. To better understand its role in health and disease, a mouse model lacking HACL1 was investigated. Under normal conditions, these mice did not display a particular phenotype. However, upon dietary administration of phytol, phytanic acid accumulated in tissues, mainly in liver and serum of KO mice. As a consequence of phytanic acid (or a metabolite) toxicity, KO mice displayed a significant weight loss, absence of abdominal white adipose tissue, enlarged and mottled liver and reduced hepatic glycogen and triglycerides. In addition, hepatic PPARα was activated. The central nervous system of the phytol-treated mice was apparently not affected. In addition, 2OH-FA did not accumulate in the central nervous system of HACL1 deficient mice, likely due to the presence in the endoplasmic reticulum of an alternate HACL1-unrelated lyase. The latter may serve as a backup system in certain tissues and account for the formation of pristanic acid in the phytol-fed KO mice. As the degradation of pristanic acid is also impaired, both phytanoyl- and pristanoyl-CoA levels are increased in liver, and the ω-oxidized metabolites are excreted in urine. In conclusion, HACL1 deficiency is not associated with a severe phenotype, but in combination with phytanic acid intake, the normal situation in man, it might present with phytanic acid elevation and resemble a Refsum like disorder.
[Mh] Termos MeSH primário: Enoil-CoA Hidratase/deficiência
Enoil-CoA Hidratase/metabolismo
Liases/metabolismo
Fitol/farmacologia
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Retículo Endoplasmático/efeitos dos fármacos
Retículo Endoplasmático/metabolismo
Ácidos Graxos/farmacologia
Feminino
Fígado/efeitos dos fármacos
Fígado/metabolismo
Masculino
Camundongos
Camundongos Knockout
Oxirredução
PPAR alfa/metabolismo
Ácido Fitânico/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids); 0 (PPAR alpha); 14721-66-5 (Phytanic Acid); 150-86-7 (Phytol); 5FMQ2908AP (pristanic acid); EC 4.- (Lyases); EC 4.2.1.17 (Enoyl-CoA Hydratase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE


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[PMID]:28617588
[Au] Autor:Babbitt SE; Hsu J; Mendez DL; Kranz RG
[Ad] Endereço:Department of Biology, Washington University , St. Louis, Missouri 63130, United States.
[Ti] Título:Biosynthesis of Single Thioether c-Type Cytochromes Provides Insight into Mechanisms Intrinsic to Holocytochrome c Synthase (HCCS).
[So] Source:Biochemistry;56(26):3337-3346, 2017 Jul 05.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:C-type cytochromes (cyts c) are generally characterized by the presence of two thioether attachments between heme and two cysteine residues within a highly conserved CXXCH motif. Most eukaryotes use the System III cyt c biogenesis pathway composed of holocytochrome c synthase (HCCS) to catalyze thioether formation. Some protozoan organisms express a functionally equivalent, natural variant of cyt c with an XXXCH heme-attachment motif, resulting in a single covalent attachment. Previous studies have shown that recombinant HCCS can produce low levels of the XXXCH single thioether variant. However, cyt c variants containing substitutions at the C-terminal cysteine of the heme-attachment site (i.e., resulting in CXXXH) have never been observed in nature, and attempts to biosynthesize a recombinant version of this cyt c variant have been largely unsuccessful. In this study, we report the biochemical analyses of an HCCS-matured CXXXH cyt c variant, comparing its biosynthesis and properties to those of the XXXCH variant. The results indicate that although HCCS mediates heme attachment to the N-terminal cysteine in CXXXH cyt c variants, up to 50% of the cyt c produced is modified in an oxygen-dependent manner, resulting in a mixed population of cyt c. Since this aerobic modification occurs only in the context of CXXXH, we also propose that natural HCCS-mediated heme attachment to CXXCH likely initiates at the C-terminal cysteine.
[Mh] Termos MeSH primário: Citocromos c/metabolismo
Liases/metabolismo
Modelos Moleculares
Engenharia de Proteínas
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sequência de Aminoácidos
Substituição de Aminoácidos
Dicroísmo Circular
Sequência Conservada
Cisteína/química
Citocromos c/química
Citocromos c/genética
Citocromos c/isolamento & purificação
Glutationa Transferase/química
Glutationa Transferase/genética
Heme/química
Seres Humanos
Liases/química
Liases/genética
Mutagênese Sítio-Dirigida
Mutação
Oxigênio/química
Conformação Proteica
Dobramento de Proteína
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/isolamento & purificação
Proteínas Recombinantes de Fusão/metabolismo
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Fusion Proteins); 42VZT0U6YR (Heme); 9007-43-6 (Cytochromes c); EC 2.5.1.18 (Glutathione Transferase); EC 4.- (Lyases); EC 4.4.1.17 (cytochrome C synthetase); K848JZ4886 (Cysteine); S88TT14065 (Oxygen)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00286


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[PMID]:28592683
[Au] Autor:Banerjee M; Chakravarty D; Ballal A
[Ad] Endereço:Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai 400 085, India manishab@barc.gov.in manisha.banerjee@gmail.com.
[Ti] Título:Molecular basis of function and the unusual antioxidant activity of a cyanobacterial cysteine desulfurase.
[So] Source:Biochem J;474(14):2435-2447, 2017 Jul 06.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cysteine desulfurases, which supply sulfur for iron-sulfur cluster biogenesis, are broadly distributed in all phyla including cyanobacteria, the progenitors of plant chloroplasts. The SUF (sulfur utilization factor) system is responsible for Fe-S cluster biosynthesis under stress. The operon from cyanobacterium PCC 7120 showed the presence of a cysteine desulfurase, ( ), but not the accessory sulfur-accepting protein (SufE). However, an open reading frame ( ) encoding a SufE-like protein (termed AsaE, sulfur acceptor E) was found at a location distinct from the operon. The purified SufS protein existed as a pyridoxal 5' phosphate (PLP)-containing dimer with a relatively low desulfurase activity. Interestingly, in the presence of the AsaE protein, the catalytic efficiency of this reaction increased 10-fold. In particular, for sulfur mobilization, the AsaE protein partnered only SufS and not other cysteine desulfurases from The SufS protein was found to physically interact with the AsaE protein, demonstrating that AsaE was indeed the missing partner of SufS. The conserved cysteine of the SufS or the AsaE protein was essential for activity but not for their physical association. Curiously, overexpression of the SufS protein in caused reduced formation of reactive oxygen species on exposure to hydrogen peroxide (H O ), resulting in superior oxidative stress tolerance to the oxidizing agent when compared with the wild-type strain. Overall, the results highlight the functional interaction between the two proteins that mediate sulfur mobilization, in the cyanobacterial SUF pathway, and further reveal that overexpression of SufS can protect cyanobacteria from oxidative stress.
[Mh] Termos MeSH primário: Anabaena/enzimologia
Proteínas de Bactérias/metabolismo
Liases de Carbono-Enxofre/metabolismo
Sulfurtransferases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Anabaena/efeitos dos fármacos
Anabaena/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biocatálise/efeitos dos fármacos
Liases de Carbono-Enxofre/química
Liases de Carbono-Enxofre/genética
Sequência Conservada
Dimerização
Farmacorresistência Bacteriana
Liases/química
Liases/genética
Liases/metabolismo
Mutagênese Sítio-Dirigida
Mutação
Fases de Leitura Aberta/efeitos dos fármacos
Óperon/efeitos dos fármacos
Oxidantes/farmacologia
Oxirredução
Estresse Oxidativo/efeitos dos fármacos
Multimerização Proteica
Fosfato de Piridoxal/metabolismo
Espécies Reativas de Oxigênio/agonistas
Espécies Reativas de Oxigênio/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Sulfurtransferases/química
Sulfurtransferases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Oxidants); 0 (Reactive Oxygen Species); 0 (Recombinant Proteins); 5V5IOJ8338 (Pyridoxal Phosphate); EC 2.8.1.- (Sulfurtransferases); EC 4.- (Lyases); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (cysteine desulfurase); EC 4.4.1.16 (selenocysteine lyase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170290


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[PMID]:28497152
[Au] Autor:Osborn AR; Kean KM; Karplus PA; Mahmud T
[Ad] Endereço:Department of Pharmaceutical Sciences, Oregon State University, Corvallis, OR 97331-3507, USA. Taifo.Mahmud@oregonstate.edu.
[Ti] Título:The sedoheptulose 7-phosphate cyclases and their emerging roles in biology and ecology.
[So] Source:Nat Prod Rep;34(8):945-956, 2017 Aug 02.
[Is] ISSN:1460-4752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Covering up to: 1999-2016This highlight covers a family of enzymes of growing importance, the sedoheptulose 7-phosphate cyclases, initially of interest due to their involvement in the biosynthesis of pharmaceutically relevant secondary metabolites. More recently, these enzymes have been found throughout Prokarya and Eukarya, suggesting their broad potential biological roles in nature.
[Mh] Termos MeSH primário: Biologia
Ecologia
Liases/metabolismo
[Mh] Termos MeSH secundário: Estrutura Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 4.- (Lyases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170513
[St] Status:MEDLINE
[do] DOI:10.1039/c7np00017k


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[PMID]:28487379
[Au] Autor:Sawicki A; Zhou S; Kwiatkowski K; Luo M; Willows RD
[Ad] Endereço:Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW 2109, Australia.
[Ti] Título:1- -histidine phosphorylation of ChlD by the AAA ChlI2 stimulates magnesium chelatase activity in chlorophyll synthesis.
[So] Source:Biochem J;474(12):2095-2105, 2017 Jun 09.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Magnesium chelatase (Mg-chelatase) inserts magnesium into protoporphyrin during the biosynthesis of chlorophyll and bacteriochlorophyll. Enzyme activity is reconstituted by forming two separate preactivated complexes consisting of a GUN4/ChlH/protoporphyrin IX substrate complex and a ChlI/ChlD enzyme 'motor' complex. Formation of the ChlI/ChlD complex in both and is accompanied by phosphorylation of ChlD by ChlI, but the orthologous protein complex from , BchI/BchD, gives no detectable phosphorylation of BchD. Phosphorylation produces a 1- -phospho-histidine within ChlD. Proteomic analysis indicates that phosphorylation occurs at a conserved His residue in the C-terminal integrin I domain of ChlD. Comparative analysis of the ChlD phosphorylation with enzyme activities of various ChlI/ChlD complexes correlates the phosphorylation by ChlI2 with stimulation of Mg-chelatase activity. Mutation of the H641 of CrChlD to E641 prevents both phosphorylation and stimulation of Mg-chelatase activity, confirming that phosphorylation at H641 stimulates Mg-chelatase. The properties of ChlI2 compared with ChlI1 of and with ChlI of , shows that ChlI2 has a regulatory role in .
[Mh] Termos MeSH primário: Chlamydomonas reinhardtii/enzimologia
Clorofila/biossíntese
Histidina Quinase/metabolismo
Liases/metabolismo
Oryza/enzimologia
Proteínas de Plantas/metabolismo
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Proteínas de Algas/agonistas
Proteínas de Algas/química
Proteínas de Algas/genética
Proteínas de Algas/metabolismo
Sequência de Aminoácidos
Substituição de Aminoácidos
Sequência Conservada
Ativação Enzimática
Estabilidade Enzimática
Histidina/metabolismo
Histidina Quinase/química
Histidina Quinase/genética
Concentração de Íons de Hidrogênio
Liases/química
Liases/genética
Mutação
Radioisótopos de Fósforo
Fosforilação
Proteínas de Plantas/agonistas
Proteínas de Plantas/química
Proteínas de Plantas/genética
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Proteômica/métodos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 0 (Phosphorus Radioisotopes); 0 (Plant Proteins); 1406-65-1 (Chlorophyll); 4QD397987E (Histidine); EC 2.7.13.1 (Histidine Kinase); EC 4.- (Lyases); EC 4.99.1- (magnesium chelatase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170511
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20161094


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[PMID]:28370935
[Au] Autor:Wang Q; Dore JE; McDermott TR
[Ad] Endereço:Department of Land Resources and Environmental Sciences, Montana State University, Bozeman, MT, 59717, USA.
[Ti] Título:Methylphosphonate metabolism by Pseudomonas sp. populations contributes to the methane oversaturation paradox in an oxic freshwater lake.
[So] Source:Environ Microbiol;19(6):2366-2378, 2017 Jun.
[Is] ISSN:1462-2920
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The 'CH oversaturation paradox' has been observed in oxygen-rich marine and lake waters, and viewed to significantly contribute to biosphere cycling of methane, a potent greenhouse gas. Our study focused on the intriguing well-defined pelagic methane enriched zone (PMEZ) in freshwater lakes. Spiking Yellowstone Lake PMEZ samples with C-labeled potential methanogenesis substrates found only C-methylphosphonate (MPn) resulted in CH generation. In 16S rRNA gene Illumina libraries, four Pseudomonas sp. operational taxonomic units surprisingly accounted for ∼11% abundance in the PMEZ community. Pseudomonas sp. isolates were also obtained from MPn enrichments with PMEZ water; they were most aggressive in MPn metabolism and their 16S rRNA gene sequences matched 35% of the Illumina PMEZ Pseudomonas reads. Further, two key genes encoding C-P lyase (phnJL, an important enzyme for dealkylation of MPn), were only amplifiable from PMEZ DNA and all PCR generated phnJL clones matched those of the Pseudomonas sp. isolates. Notably, methanogen 16S rRNA signatures were absent in all Illumina libraries and mcrA was not detected via PCR. Collectively, these observations are consistent with the conclusion that MPn metabolism contributes significantly to CH oversaturation in Yellowstone Lake and likely other oxic freshwater lake environments, and that Pseudomonas sp. populations are critical participants.
[Mh] Termos MeSH primário: Lagos/química
Metano/metabolismo
Compostos Organofosforados/metabolismo
Pseudomonas/metabolismo
[Mh] Termos MeSH secundário: Enzimas de Restrição do DNA/genética
Euryarchaeota/genética
Lagos/microbiologia
Liases/genética
Filogenia
RNA Ribossômico 16S/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Organophosphorus Compounds); 0 (RNA, Ribosomal, 16S); 329W4YM10Z (methylphosphonic acid); EC 3.1.21.- (DNA Restriction Enzymes); EC 3.1.21.- (endodeoxyribonuclease McrA); EC 4.- (Lyases); EC 4.99.- (carbon-phosphorus lyase); OP0UW79H66 (Methane)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1111/1462-2920.13747


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[PMID]:28361363
[Au] Autor:Xu P; Gao J; Cao Z; Chee PW; Guo Q; Xu Z; Paterson AH; Zhang X; Shen X
[Ad] Endereço:Key Laboratory of Cotton and Rapeseed (Nanjing), Ministry of Agriculture, Nanjing, People's Republic of China.
[Ti] Título:Fine mapping and candidate gene analysis of qFL-chr1, a fiber length QTL in cotton.
[So] Source:Theor Appl Genet;130(6):1309-1319, 2017 Jun.
[Is] ISSN:1432-2242
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: A fiber length QTL, qFL-chr1, was fine mapped to a 0.9 cM interval of cotton chromosome 1. Two positional candidate genes showed positive correlation between gene expression level and fiber length. Prior analysis of a backcross-self mapping population derived from a cross between Gossypium hirsutum L. and G. barbadense L. revealed a QTL on chromosome 1 associated with increased fiber length (qFL-chr1), which was confirmed in three independent populations of near-isogenic introgression lines (NIILs). Here, a single NIIL, R01-40-08, was used to develop a large population segregating for the target region. Twenty-two PCR-based polymorphic markers used to genotype 1672 BC F plants identified 432 recombinants containing breakpoints in the target region. Substitution mapping using 141 informative recombinants narrowed the position of qFL-chr1 to a 1.0-cM interval between SSR markers MUSS084 and CIR018. To exclude possible effects of non-target introgressions on fiber length, different heterozygous BC F plants introgressed between SSR markers NAU3384 and CGR5144 were selected to develop sub-NILs. The qFL-chr1 was further mapped at 0.9-cM interval between MUSS422 and CIR018 by comparisons of sub-NIL phenotype, and increased fiber length by ~1 mm. The 2.38-Mb region between MUSS422 and CIR018 in G. barbadense contained 19 annotated genes. Expression levels of two of these genes, GOBAR07705 (encoding 1-aminocyclopropane-1-carboxylate synthase) and GOBAR25992 (encoding amino acid permease), were positively correlated with fiber length in a small F population, supporting these genes as candidates for qFL-chr1.
[Mh] Termos MeSH primário: Mapeamento Cromossômico
Fibra de Algodão
Gossypium/genética
Locos de Características Quantitativas
[Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos/genética
Genes de Plantas
Marcadores Genéticos
Genótipo
Liases/genética
Fenótipo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Genetic Markers); EC 4.- (Lyases); EC 4.4.1.14 (1-aminocyclopropanecarboxylate synthase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170917
[Lr] Data última revisão:
170917
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE
[do] DOI:10.1007/s00122-017-2890-8


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[PMID]:28323419
[Au] Autor:Bühning M; Valleriani A; Leimkühler S
[Ad] Endereço:Institute of Biochemistry and Biology, University of Potsdam , D-14476 Potsdam, Germany.
[Ti] Título:The Role of SufS Is Restricted to Fe-S Cluster Biosynthesis in Escherichia coli.
[So] Source:Biochemistry;56(14):1987-2000, 2017 Apr 11.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In Escherichia coli, two different systems that are important for the coordinate formation of Fe-S clusters have been identified, namely, the ISC and SUF systems. The ISC system is the housekeeping Fe-S machinery, which provides Fe-S clusters for numerous cellular proteins. The IscS protein of this system was additionally revealed to be the primary sulfur donor for several sulfur-containing molecules with important biological functions, among which are the molybdenum cofactor (Moco) and thiolated nucleosides in tRNA. Here, we show that deletion of central components of the ISC system in addition to IscS leads to an overall decrease in Fe-S cluster enzyme and molybdoenzyme activity in addition to a decrease in the number of Fe-S-dependent thiomodifications of tRNA, based on the fact that some proteins involved in Moco biosynthesis and tRNA thiolation are Fe-S-dependent. Complementation of the ISC deficient strains with the suf operon restored the activity of Fe-S-containing proteins, including the MoaA protein, which is involved in the conversion of 5'GTP to cyclic pyranopterin monophosphate in the fist step of Moco biosynthesis. While both systems share a high degree of similarity, we show that the function of their respective l-cysteine desulfurase IscS or SufS is specific for each cellular pathway. It is revealed that SufS cannot play the role of IscS in sulfur transfer for the formation of 2-thiouridine, 4-thiouridine, or the dithiolene group of molybdopterin, being unable to interact with TusA or ThiI. The results demonstrate that the role of the SUF system is exclusively restricted to Fe-S cluster assembly in the cell.
[Mh] Termos MeSH primário: Liases de Carbono-Enxofre/metabolismo
Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Proteínas com Ferro-Enxofre/metabolismo
Liases/metabolismo
[Mh] Termos MeSH secundário: Liases de Carbono-Enxofre/genética
Coenzimas/biossíntese
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Proteínas com Ferro-Enxofre/genética
Isomerases/genética
Isomerases/metabolismo
Liases/genética
Metaloproteínas/biossíntese
Óperon
Pteridinas
RNA de Transferência/genética
RNA de Transferência/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Sulfurtransferases/genética
Sulfurtransferases/metabolismo
Tiouridina/análogos & derivados
Tiouridina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2-thiouridine); 0 (Coenzymes); 0 (Escherichia coli Proteins); 0 (Iron-Sulfur Proteins); 0 (Metalloproteins); 0 (Pteridines); 0 (Recombinant Proteins); 0 (TusA protein, E coli); 13957-31-8 (Thiouridine); 73508-07-3 (molybdenum cofactor); 9014-25-9 (RNA, Transfer); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.- (thiI protein, E coli); EC 4.- (Lyases); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (cysteine desulfurase); EC 4.4.1.16 (selenocysteine lyase); EC 5.- (Isomerases); EC 5.- (MoaA protein, E coli)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00040



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