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[PMID]:29409851
[Au] Autor:Tan M; Li G; Qi S; Liu X; Chen X; Ma J; Zhang D; Han M
[Ad] Endereço:College of Horticulture, Northwest A & F University, Yangling, Shaanxi 712100, China.
[Ti] Título:Identification and expression analysis of the IPT and CKX gene families during axillary bud outgrowth in apple (Malus domestica Borkh.).
[So] Source:Gene;651:106-117, 2018 Apr 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Cytokinins (CKs) play a crucial role in promoting axillary bud outgrowth and targeting the control of CK metabolism can be used to enhance branching in plants. CK levels are maintained mainly by CK biosynthesis (isopentenyl transferase, IPT) and degradation (dehydrogenase, CKX) genes in plants. A systematic study of the IPT and CKX gene families in apple, however, has not been conducted. In the present study, 12 MdIPTs and 12 MdCKXs were identified in the apple genome. Systematic phylogenetic, structural, and synteny analyses were performed. Expression analysis of these genes in different tissues was also assessed. MdIPT and MdCKX genes exhibit distinct expression patterns in different tissues. The response of MdIPT, MdCKX, and MdPIN1 genes to various treatments (6-BA, decapitation and Lovastatin, an inhibitor of CKs synthesis) that impact branching were also investigated. Results indicated that most of the MdIPT and MdCKX, and MdPIN1 genes were upregulated by 6-BA and decapitation treatment, but inhibited by Lovastatin, a compound that effectively suppresses axillary bud outgrowth induced by decapitation. These findings suggest that cytokinin biosynthesis is required for the activation of bud break and the export of auxin from buds in apple tree with intact primary shoot apex or decapitated apple tree. MdCKX8 and MdCKX10, however, exhibited little response to decapitation, but were significantly up-regulated by 6-BA and Lovastatin, a finding that warrants further investigation in order to understand their function in bud-outgrowth.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/genética
Genes de Plantas
Malus/genética
Oxirredutases/genética
[Mh] Termos MeSH secundário: Arabidopsis/genética
Compostos de Benzil/farmacologia
Mapeamento Cromossômico
Cromossomos de Plantas
Evolução Molecular
Flores/genética
Perfilação da Expressão Gênica
Regulação da Expressão Gênica de Plantas
Genoma de Planta
Lovastatina/farmacologia
Malus/enzimologia
Malus/crescimento & desenvolvimento
Família Multigênica
Filogenia
Reguladores de Crescimento de Planta
Purinas/farmacologia
Sintenia
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzyl Compounds); 0 (Plant Growth Regulators); 0 (Purines); 9LHU78OQFD (Lovastatin); EC 1.- (Oxidoreductases); EC 1.5.99.12 (cytokinin oxidase); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.27 (adenylate isopentenyltransferase); KXG6A989PS (benzylaminopurine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180208
[St] Status:MEDLINE


  2 / 4019 MEDLINE  
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[PMID]:28471404
[Au] Autor:Aubee JI; Olu M; Thompson KM
[Ad] Endereço:Department of Microbiology, College of Medicine, Howard University, Washington, DC 20059, USA. joseph.aubee@howard.edu.
[Ti] Título:TrmL and TusA Are Necessary for rpoS and MiaA Is Required for hfq Expression in Escherichia coli.
[So] Source:Biomolecules;7(2), 2017 May 04.
[Is] ISSN:2218-273X
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Previous work demonstrated that efficient RNA Polymerase sigma S-subunit (RpoS) translation requires the N6-isopentenyladenosine i6A37 transfer RNA (tRNA) modification for UUX-Leu decoding. Here we investigate the effect of two additional tRNA modification systems on RpoS translation; the analysis was also extended to another High UUX-leucine codon (HULC) protein, Host Factor for phage Qß (Hfq). One tRNA modification, the addition of the 2'-O-methylcytidine/uridine 34 (C/U34m) tRNA modification by tRNA (cytidine/uridine-2'O)-ribose methyltransferase L (TrmL), requires the presence of the 6-isopentenyladenosine 37 (i6A37) and therefore it seemed possible that the defect in RpoS translation in the absence of i6A37 prenyl transferase (MiaA) was in fact due to the inability to add the C/U34m modification to UUX-Leu tRNAs. The second modification, addition of 2-thiouridine (s²U), part of (mnm5s²U34), is dependent on tRNA 2-thiouridine synthesizing protein A (TusA), previously shown to affect RpoS levels. We compared expression of P - translational fusions carrying wild-type UUX leucine codons with derivatives in which UUX codons were changed to CUX codons, in the presence and absence of TrmL or TusA. The absence of these proteins, and therefore presumably the modifications they catalyze, both abolished P - - translation activity. UUX-Leu to CUX-Leu codon mutations in suppressed the requirement for P - - expression. Thus, it is likely that the C/U34m and s²U34 tRNA modifications are necessary for full translation. We also measured P - translational fusion activity in the absence of C/U34m ( ) or i6A37 ( ). The absence of i6A37 resulted in decreased P - expression, consistent with a role for i6A37 tRNA modification for translation.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/metabolismo
Proteínas de Bactérias/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Fator Proteico 1 do Hospedeiro/genética
Metiltransferases/metabolismo
Fator sigma/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Escherichia coli/genética
RNA de Transferência/genética
RNA de Transferência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 0 (Hfq protein, E coli); 0 (Host Factor 1 Protein); 0 (Sigma Factor); 0 (TusA protein, E coli); 0 (sigma factor KatF protein, Bacteria); 9014-25-9 (RNA, Transfer); EC 2.1.1.- (Methyltransferases); EC 2.1.1.- (TrmL protein, E coli); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.27 (adenylate isopentenyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  3 / 4019 MEDLINE  
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[PMID]:29355496
[Au] Autor:Lee S; Cheung-See-Kit M; Williams TA; Yamout N; Zufferey R
[Ad] Endereço:Department of Biological Sciences, St John's University, 8000 Utopia Parkway, Jamaica, NY 11439, USA.
[Ti] Título:The glycosomal alkyl-dihydroxyacetonephosphate synthase TbADS is essential for the synthesis of ether glycerophospholipids in procyclic trypanosomes.
[So] Source:Exp Parasitol;185:71-78, 2018 Feb.
[Is] ISSN:1090-2449
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycerophospholipids are the main constituents of the biological membranes in Trypanosoma brucei, which causes sleeping sickness in humans. The present work reports the characterization of the alkyl-dihydroxyacetonephosphate synthase TbADS that catalyzes the committed step in ether glycerophospholipid biosynthesis. TbADS localizes to the glycosomal lumen. TbADS complemented a null mutant of Leishmania major lacking alkyl-dihydroxyacetonephosphate synthase activity and restored the formation of normal form of the ether lipid based virulence factor lipophosphoglycan. Despite lacking alkyl-dihydroxyacetonephosphate synthase activity, a null mutant of TbADS in procyclic trypanosomes remained viable and exhibited normal growth. Comprehensive analysis of cellular glycerophospholipids showed that TbADS was involved in the biosynthesis of all ether glycerophospholipid species, primarily found in the PE and PC classes.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/metabolismo
Glicerofosfolipídeos/biossíntese
Leishmania major/enzimologia
Microcorpos/enzimologia
Trypanosoma brucei brucei/enzimologia
[Mh] Termos MeSH secundário: Leishmania major/genética
Leishmania major/metabolismo
Mutação com Perda de Função
Plasmídeos/química
Plasmídeos/genética
Plasmídeos/metabolismo
Espectrometria de Massas em Tandem
Trypanosoma brucei brucei/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycerophospholipids); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.26 (alkylglycerone-phosphate synthase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180123
[St] Status:MEDLINE


  4 / 4019 MEDLINE  
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[PMID]:29248443
[Au] Autor:Jin Z; Kwon M; Lee AR; Ro DK; Wungsintaweekul J; Kim SU
[Ad] Endereço:Department of Agricultural Biotechnology and Research Institute for Agricultural Sciences, Seoul National University, Seoul 08826, Republic of Korea.
[Ti] Título:Molecular cloning and functional characterization of three terpene synthases from unripe fruit of black pepper (Piper nigrum).
[So] Source:Arch Biochem Biophys;638:35-40, 2018 01 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To identify terpene synthases (TPS) responsible for the biosynthesis of the sesquiterpenes that contribute to the characteristic flavors of black pepper (Piper nigrum), unripe peppercorn was subjected to the Illumina transcriptome sequencing. The BLAST analysis using amorpha-4,11-diene synthase as a query identified 19 sesquiterpene synthases (sesqui-TPSs), of which three full-length cDNAs (PnTPS1 through 3) were cloned. These sesqui-TPS cDNAs were expressed in E. coli to produce recombinant enzymes for in vitro assays, and also expressed in the engineered yeast strain to assess their catalytic activities in vivo. PnTPS1 produced ß-caryophyllene as a main product and humulene as a minor compound, and thus was named caryophyllene synthase (PnCPS). Likewise, PnTPS2 and PnTPS3 were, respectively, named cadinol/cadinene synthase (PnCO/CDS) and germacrene D synthase (PnGDS). PnGDS expression in yeast yielded ß-cadinene and α-copaene, the rearrangement products of germacrene D. Their k /K values (20-37.7 s mM ) were comparable to those of other sesqui-TPSs. Among three PnTPSs, the transcript level of PnCPS was the highest, correlating with the predominant ß-caryophyllene biosynthesis in the peppercorn. The products and rearranged products of three PnTPSs could account for about a half of the sesquiterpenes in number found in unripe peppercorn.
[Mh] Termos MeSH primário: Alquil e Aril Transferases
Clonagem Molecular
Frutas
Piper nigrum
Proteínas de Plantas
[Mh] Termos MeSH secundário: Alquil e Aril Transferases/genética
Alquil e Aril Transferases/metabolismo
DNA Complementar/genética
Frutas/enzimologia
Frutas/genética
Piper nigrum/enzimologia
Piper nigrum/genética
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Sesquiterpenos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Complementary); 0 (Plant Proteins); 0 (Sesquiterpenes); 54W56MD2WD (humulene); BHW853AU9H (caryophyllene); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (terpene synthase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171218
[St] Status:MEDLINE


  5 / 4019 MEDLINE  
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[PMID]:29196256
[Au] Autor:Yang D; Fang Y; Xia P; Zhang X; Liang Z
[Ad] Endereço:Key Laboratory of Plant Secondary Metabolism and Regulation of Zhejiang Province, College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou, China.
[Ti] Título:Diverse responses of tanshinone biosynthesis to biotic and abiotic elicitors in hairy root cultures of Salvia miltiorrhiza and Salvia castanea Diels f. tomentosa.
[So] Source:Gene;643:61-67, 2018 Feb 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Salvia miltiorrhiza (S. miltiorrhiza) and Salvia castanea Diels f. tomentosa (S. castanea) are both used for treatment of cardiovascular diseases. They have the same bioactive compound tanshinones, but whose contents are hugely different. This study illustrated diverse responses of tanshinone biosynthesis to yeast extract (YE) and Ag in hairy roots of the two species. YE enhanced both the growth and tanshinone biosynthesis of two hairy roots, and contributed more to tanshinone accumulation in S. castanea than that in S. miltiorrhiza. Genes encoding 1-deoxy-d-xylulose 5-phosphate synthase (DXS2), geranylgeranyl diphosphatesynthase (GGPPS1), copalyl diphosphate synthase (CPS1), and two cytochromes P450 (CYP76AH1 and CYP76AH3) were also more responsive to YE in S. castanea than those in S. miltiorrhiza. Accumulations of dihydrotanshinone I and tanshinone I, and most biosynthetic genes in S. miltiorrhiza were more responsive to Ag than those in S. castanea. Accumulations of dihydrotanshinone I and cryptotanshinone were more responsive to YE, while tanshinone IIA accumulation was more responsive to Ag in S. miltiorrhiza. However, accumulations of other four tanshinones and related genes in S. castanea were more responsive to YE than Ag . This study provides foundations for studying diverse specialized metabolism between the related species.
[Mh] Termos MeSH primário: Diterpenos Abietanos/biossíntese
Salvia miltiorrhiza/genética
Salvia miltiorrhiza/metabolismo
[Mh] Termos MeSH secundário: Alquil e Aril Transferases/genética
Alquil e Aril Transferases/metabolismo
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/metabolismo
Farnesiltranstransferase/genética
Farnesiltranstransferase/metabolismo
Regulação da Expressão Gênica de Plantas/genética
Medicina Tradicional Chinesa
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Raízes de Plantas/metabolismo
Salvia/genética
Prata/metabolismo
Transferases/genética
Transferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Diterpenes, Abietane); 0 (Plant Proteins); 03UUH3J385 (tanshinone); 3M4G523W1G (Silver); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 2.- (Transferases); EC 2.2.1.- (deoxyxylulose-5-phosphate synthase); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (ent-kaurene synthetase A); EC 2.5.1.29 (Farnesyltranstransferase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180123
[Lr] Data última revisão:
180123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171203
[St] Status:MEDLINE


  6 / 4019 MEDLINE  
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[PMID]:29190729
[Au] Autor:Tan Z; Jia X; Ma F; Feng Y; Lu H; Jin JO; Wu D; Yin L; Liu L; Zhang L
[Ad] Endereço:Shanghai Public Health Clinical Center, Fudan University, Shanghai, China.
[Ti] Título:Increased MMAB level in mitochondria as a novel biomarker of hepatotoxicity induced by Efavirenz.
[So] Source:PLoS One;12(11):e0188366, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Efavirenz (EFV), a non-nucleoside reverse transcriptase inhibitor (NNRTI), has been widely used in the therapy of human immunodeficiency virus (HIV) infection. Some of its toxic effects on hepatic cells have been reported to display features of mitochondrial dysfunction through bioenergetic stress and autophagy, etc. However, alteration of protein levels, especially mitochondrial protein levels, in hepatic cells during treatment of EFV has not been fully investigated. METHODS: We built a cell model of EFV-induced liver toxicity through treating Huh-7 cells with different concentrations of EFV for different time followed by the analysis of cell viability using cell counting kit -8 (CCK8) and reactive oxygen species (ROS) using 2',7'-dichlorodihydrofluorescein diacetate (DCFH-DA) and MitoSox dye. Proteomic profiles in the mitochondria of Huh-7 cells stimulated by EFV were analyzed. Four differentially expressed proteins were quantified by real time RT-PCR. We also detected the expression of mitochondrial precursor Cob(I)yrinic acid a,c-diamide adenosyltransferase (MMAB) by immunohistochemistry analysis in clinical samples. The expression levels of MMAB and ROS were detected in EFV-treated Huh-7 cells with and without shRNA used to knock down MMAB, and in primary hepatocytes (PHC). The effects of other anti-HIV drugs (nevirapine (NVP) and tenofovirdisoproxil (TDF)), and hydrogen peroxide (H2O2) were also tested. Amino acid analysis and fatty aldehyde dehydrogenase (ALDH3A2) expression after MMAB expression knock-down with shRNA was used to investigate the metabolic effect of MMAB in Huh-7 cells. RESULTS: EFV treatment inhibited cell viability and increased ROS production with time- and concentration-dependence. Proteomic study was performed at 2 hours after EFV treatment. After treated Huh-7 cells with EFV (2.5mg/L or 10 mg/L) for 2 h, fifteen differentially expressed protein spots from purified mitochondrion that included four mitochondria proteins were detected in EFV-treated Huh-7 cells compared to controls. Consistent with protein expression levels, mRNA expression levels of mitochondrial protein MMAB were also increased by EFV treatment. In addition, the liver of EFV-treated HIV infected patients showed substantially higher levels of MMAB expression compared to the livers of untreated or protease inhibitor (PI)-treated HIV-infected patients. Furthermore, ROS were found to be decreased in Huh-7 cells treated with shMMAB compared with empty plasmid treated with EFV at the concentration of 2.5 or 10 mg/L. MMAB was increased in EFV-treated Huh-7 cells and primary hepatocytes. However, no change in MMAB expression was detected after treatment of Huh-7 cells and primary hepatocytes with anti-HIV drugs nevirapine (NVP) and tenofovirdisoproxil (TDF), or hydrogen peroxide (H2O2), although ROS was increased in these cells. Finally, knockdown of MMAB by shRNA induced increases in the ß-Alanine (ß-Ala) production levels and decrease in ALDH3A2 expression. CONCLUSIONS: A mitochondrial proteomic study was performed to study the proteins related to EFV-inducted liver toxicity. MMAB might be a target and potential biomarker of hepatotoxicity in EFV-induced liver toxicity.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/metabolismo
Benzoxazinas/toxicidade
Mitocôndrias/enzimologia
Inibidores da Transcriptase Reversa/farmacologia
[Mh] Termos MeSH secundário: Aldeído Desidrogenase/genética
Alquil e Aril Transferases/genética
Western Blotting
Linhagem Celular
Perfilação da Expressão Gênica
Técnicas de Silenciamento de Genes
Seres Humanos
Fígado/efeitos dos fármacos
Fígado/metabolismo
Proteínas Mitocondriais/genética
Estresse Oxidativo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Transcrição Genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoxazines); 0 (Mitochondrial Proteins); 0 (Reverse Transcriptase Inhibitors); EC 1.2.1.3 (Aldehyde Dehydrogenase); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.17 (cob(I)alamin adenosyltransferase); JE6H2O27P8 (efavirenz)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188366


  7 / 4019 MEDLINE  
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[PMID]:28842490
[Au] Autor:Grabinska KA; Edani BH; Park EJ; Kraehling JR; Sessa WC
[Ad] Endereço:From the Department of Pharmacology and Vascular Biology and Therapeutics Program, Yale University School of Medicine, New Haven, Connecticut 06520.
[Ti] Título:A conserved C-terminal R G motif in the NgBR subunit of -prenyltransferase is critical for prenyltransferase activity.
[So] Source:J Biol Chem;292(42):17351-17361, 2017 Oct 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:-Prenyltransferases ( -PTs) constitute a large family of enzymes conserved during evolution and present in all domains of life. In eukaryotes and archaea, -PT is the first enzyme committed to the synthesis of dolichyl phosphate, an obligate lipid carrier in protein glycosylation reactions. The homodimeric bacterial enzyme, undecaprenyl diphosphate synthase, generates 11 isoprene units and has been structurally and mechanistically characterized in great detail. Recently, we discovered that unlike undecaprenyl diphosphate synthase, mammalian -PT is a heteromer consisting of NgBR (Nus1) and hCIT (dehydrodolichol diphosphate synthase) subunits, and this composition has been confirmed in plants and fungal -PTs. Here, we establish the first purification system for heteromeric -PT and show that both NgBR and hCIT subunits function in catalysis and substrate binding. Finally, we identified a critical R G sequence in the C-terminal tail of NgBR that is conserved and essential for enzyme activity across phyla. In summary, our findings show that eukaryotic -PT is composed of the NgBR and hCIT subunits. The strong conservation of the R G motif among NgBR orthologs indicates that this subunit is critical for the synthesis of polyprenol diphosphates and cellular function.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/química
Dimetilaliltranstransferase/química
Receptores de Superfície Celular/química
Transferases/química
[Mh] Termos MeSH secundário: Alquil e Aril Transferases/genética
Alquil e Aril Transferases/metabolismo
Motivos de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Dimetilaliltranstransferase/genética
Dimetilaliltranstransferase/metabolismo
Proteínas Fúngicas/química
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Seres Humanos
Proteínas de Plantas/química
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Receptores de Superfície Celular/genética
Receptores de Superfície Celular/metabolismo
Transferases/genética
Transferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fungal Proteins); 0 (NUS1 protein, human); 0 (Plant Proteins); 0 (Receptors, Cell Surface); EC 2.- (Transferases); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (cis-prenyl transferase); EC 2.5.1.- (dehydrodolichyl diphosphate synthetase); EC 2.5.1.1 (Dimethylallyltranstransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170827
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.806034


  8 / 4019 MEDLINE  
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[PMID]:28841019
[Au] Autor:Christianson DW
[Ad] Endereço:Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania , 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, United States.
[Ti] Título:Structural and Chemical Biology of Terpenoid Cyclases.
[So] Source:Chem Rev;117(17):11570-11648, 2017 Sep 13.
[Is] ISSN:1520-6890
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The year 2017 marks the twentieth anniversary of terpenoid cyclase structural biology: a trio of terpenoid cyclase structures reported together in 1997 were the first to set the foundation for understanding the enzymes largely responsible for the exquisite chemodiversity of more than 80000 terpenoid natural products. Terpenoid cyclases catalyze the most complex chemical reactions in biology, in that more than half of the substrate carbon atoms undergo changes in bonding and hybridization during a single enzyme-catalyzed cyclization reaction. The past two decades have witnessed structural, functional, and computational studies illuminating the modes of substrate activation that initiate the cyclization cascade, the management and manipulation of high-energy carbocation intermediates that propagate the cyclization cascade, and the chemical strategies that terminate the cyclization cascade. The role of the terpenoid cyclase as a template for catalysis is paramount to its function, and protein engineering can be used to reprogram the cyclization cascade to generate alternative and commercially important products. Here, I review key advances in terpenoid cyclase structural and chemical biology, focusing mainly on terpenoid cyclases and related prenyltransferases for which X-ray crystal structures have informed and advanced our understanding of enzyme structure and function.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/química
Terpenos/metabolismo
[Mh] Termos MeSH secundário: Alquil e Aril Transferases/metabolismo
Carbono-Carbono Liases/química
Carbono-Carbono Liases/metabolismo
Cristalografia por Raios X
Dimetilaliltranstransferase/química
Dimetilaliltranstransferase/metabolismo
Liases Intramoleculares/química
Liases Intramoleculares/metabolismo
Estrutura Terciária de Proteína
Terpenos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Terpenes); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (terpene carbocyclase); EC 2.5.1.1 (Dimethylallyltranstransferase); EC 4.1.- (Carbon-Carbon Lyases); EC 4.2.3.6 (trichodiene synthetase); EC 5.5.- (Intramolecular Lyases); EC 5.5.- (pinene cyclase I)
[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:170826
[St] Status:MEDLINE
[do] DOI:10.1021/acs.chemrev.7b00287


  9 / 4019 MEDLINE  
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[PMID]:28701463
[Au] Autor:Kries H; Kellner F; Kamileen MO; O'Connor SE
[Ad] Endereço:From the Department of Biological Chemistry, The John Innes Centre, Norwich NR4 7UH, United Kingdom and.
[Ti] Título:Inverted stereocontrol of iridoid synthase in snapdragon.
[So] Source:J Biol Chem;292(35):14659-14667, 2017 Sep 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The natural product class of iridoids, found in various species of flowering plants, harbors astonishing chemical complexity. The discovery of iridoid biosynthetic genes in the medicinal plant has provided insight into the biosynthetic origins of this class of natural product. However, not all iridoids share the exact five- to six-bicyclic ring scaffold of the iridoids. For instance, iridoids in the ornamental flower snapdragon ( , Plantaginaceae family) are derived from the C7 epimer of this scaffold. Here we have cloned and characterized the iridoid synthase enzyme from (AmISY), the enzyme that is responsible for converting 8-oxogeranial into the bicyclic iridoid scaffold in a two-step reduction-cyclization sequence. Chiral analysis of the reaction products reveals that AmISY reduces C7 to generate the opposite stereoconfiguration in comparison with the homologue CrISY. The catalytic activity of AmISY thus explains the biosynthesis of 7-epi-iridoids in and related genera. However, although the stereoselectivity of the reduction step catalyzed by AmISY is clear, in both AmISY and CrISY, the cyclization step produces a diastereomeric mixture. Although the reduction of 8-oxogeranial is clearly enzymatically catalyzed, the cyclization step appears to be subject to less stringent enzyme control.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/metabolismo
Antirrhinum/enzimologia
Iridoides/metabolismo
Modelos Moleculares
Proteínas de Plantas/metabolismo
[Mh] Termos MeSH secundário: Alquil e Aril Transferases/química
Alquil e Aril Transferases/genética
Substituição de Aminoácidos
Biocatálise
Domínio Catalítico
Catharanthus/enzimologia
Iridoides/química
Estrutura Molecular
Monoterpenos/química
Monoterpenos/metabolismo
Mutação
NADP/química
NADP/metabolismo
Oxirredução
Filogenia
Proteínas de Plantas/química
Proteínas de Plantas/genética
Conformação Proteica
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Estereoisomerismo
Homologia Estrutural de Proteína
Especificidade por Substrato
Terpenos/química
Terpenos/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iridoids); 0 (Monoterpenes); 0 (Plant Proteins); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (Terpenes); 53-59-8 (NADP); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (terpene synthase); PL902IKN0A (decaprenoic acid); T7EU0O9VPP (citral)
[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:170714
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.800979


  10 / 4019 MEDLINE  
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[PMID]:28628628
[Au] Autor:Nelson SK; Steber CM
[Ad] Endereço:Molecular Plant Sciences Program, Washington State University, Pullman, Washington, United States of America.
[Ti] Título:Transcriptional mechanisms associated with seed dormancy and dormancy loss in the gibberellin-insensitive sly1-2 mutant of Arabidopsis thaliana.
[So] Source:PLoS One;12(6):e0179143, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:While widespread transcriptome changes were previously observed with seed dormancy loss, this study specifically characterized transcriptional changes associated with the increased seed dormancy and dormancy loss of the gibberellin (GA) hormone-insensitive sleepy1-2 (sly1-2) mutant. The SLY1 gene encodes the F-box subunit of an SCF E3 ubiquitin ligase needed for GA-triggered proteolysis of DELLA repressors of seed germination. DELLA overaccumulation in sly1-2 seeds leads to increased dormancy that can be rescued without DELLA protein destruction either by overexpression of the GA receptor, GA-INSENSITIVE DWARF1b (GID1b-OE) (74% germination) or by extended dry after-ripening (11 months, 51% germination). After-ripening of sly1 resulted in different transcriptional changes in early versus late Phase II of germination that were consistent with the processes known to occur. Approximately half of the transcriptome changes with after-ripening appear to depend on SLY1-triggered DELLA proteolysis. Given that many of these SLY1/GA-dependent changes are genes involved in protein translation, it appears that GA signaling increases germination capacity in part by activating translation. While sly1-2 after-ripening was associated with transcript-level changes in 4594 genes over two imbibition timepoints, rescue of sly1-2 germination by GID1b-OE was associated with changes in only 23 genes. Thus, a big change in sly1-2 germination phenotype can occur with relatively little change in the global pattern of gene expression during the process of germination. Most GID1b-OE-responsive transcripts showed similar changes with after-ripening in early Phase II of imbibition, but opposite changes with after-ripening by late Phase II. This suggests that GID1b-OE stimulates germination early in imbibition, but may later trigger negative feedback regulation.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/metabolismo
Proteínas de Arabidopsis/metabolismo
Arabidopsis/efeitos dos fármacos
Giberelinas/farmacologia
Dormência de Plantas/efeitos dos fármacos
Transcriptoma/efeitos dos fármacos
[Mh] Termos MeSH secundário: Alquil e Aril Transferases/genética
Arabidopsis/genética
Arabidopsis/crescimento & desenvolvimento
Proteínas de Arabidopsis/genética
Germinação/efeitos dos fármacos
Mutação
Fenótipo
Reguladores de Crescimento de Planta/farmacologia
Plantas Geneticamente Modificadas/metabolismo
Proteólise
RNA de Plantas/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Receptores de Superfície Celular/genética
Receptores de Superfície Celular/metabolismo
Sementes/efeitos dos fármacos
Sementes/genética
Sementes/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (GAI protein, Arabidopsis); 0 (GID1b protein, Arabidopsis); 0 (Gibberellins); 0 (Plant Growth Regulators); 0 (RNA, Plant); 0 (Receptors, Cell Surface); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.29 (SLY1 protein, Arabidopsis)
[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:170620
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179143



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