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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


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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


  3 / 7046 MEDLINE  
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[PMID]:28591487
[Au] Autor:Lee M; Hesek D; Lastochkin E; Dik DA; Boggess B; Mobashery S
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, USA.
[Ti] Título:Deciphering the Nature of Enzymatic Modifications of Bacterial Cell Walls.
[So] Source:Chembiochem;18(17):1696-1702, 2017 Sep 05.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The major constituent of bacterial cell walls is peptidoglycan, which, in its crosslinked form, is a polymer of considerable complexity that encases the entire bacterium. A functional cell wall is indispensable for survival of the organism. There are several dozen enzymes that assemble and disassemble the peptidoglycan dynamically within each bacterial generation. Understanding of the nature of these transformations is critical knowledge for these events. Octasaccharide peptidoglycans were prepared and studied with seven recombinant cell-wall-active enzymes (SltB1, MltB, RlpA, mutanolysin, AmpDh2, AmpDh3, and PBP5). With the use of highly sensitive mass spectrometry methods, we described the breadth of reactions that these enzymes catalyzed with peptidoglycan and shed light on the nature of the cell wall alteration performed by these enzymes. The enzymes exhibit broadly distinct preferences for their substrate peptidoglycans in the reactions that they catalyze.
[Mh] Termos MeSH primário: Bactérias/metabolismo
Parede Celular/metabolismo
Enzimas/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Cromatografia Líquida de Alta Pressão
Endopeptidases/genética
Endopeptidases/metabolismo
Enzimas/genética
Glicosídeo Hidrolases/genética
Glicosídeo Hidrolases/metabolismo
Espectrometria de Massas
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/metabolismo
Peptidoglicano/análise
Peptidoglicano/química
Peptidoglicano/metabolismo
Pseudomonas aeruginosa/enzimologia
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Streptomyces griseus/enzimologia
Especificidade por Substrato
Transferases/genética
Transferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes); 0 (Multienzyme Complexes); 0 (Peptidoglycan); 0 (Recombinant Proteins); 0 (transglycosidase enzyme system); EC 2.- (Transferases); EC 3.2.1.- (Glycoside Hydrolases); EC 3.4.- (Endopeptidases); EC 3.4.99.- (mutanolysin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170608
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700293


  4 / 7046 MEDLINE  
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[PMID]:28481197
[Au] Autor:Szczuka E; Jablonska L; Kaznowski A
[Ad] Endereço:Department of Microbiology, Institute of Experimental Biology, Faculty of Biology, Adam Mickiewicz University, Poznan, Poland.
[Ti] Título:Effect of subinhibitory concentrations of tigecycline and ciprofloxacin on the expression of biofilm-associated genes and biofilm structure of Staphylococcus epidermidis.
[So] Source:Microbiology;163(5):712-718, 2017 May.
[Is] ISSN:1465-2080
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Staphylococcus epidermidis is a leading cause of foreign body-associated infections. This is related to the bacterium's ability to form biofilms on synthetic materials. Bacteria within a biofilm may be exposed to subinhibitory concentrations (sub-MICs) of antibiotics because of an agent's limited penetration into the biofilm core. Here, we investigated the effect of sub-MICs of tigecycline and ciprofloxacin on the expression of biofilm-associated genes, i.e. icaA, altE and sigB, and the biofilm structure of five clinical isolates of S. epidermidis. For most tested isolates, the expression of these genes increased after exposure to 0.25 MIC and 0.5 MIC tigecycline. A slight decrease in icaAmRNA levels was observed only in two isolates in the presence of 0.25 MIC tigecycline. The effect of ciprofloxacin exposure was isolate-dependent. At 0.5 MIC, ciprofloxacin induced an increase of sigB and icaAmRNA levels in three of the five tested isolates. At the same time, expression of the altE gene increased in all isolates (from 1.3-fold to 42-fold, depending on the strain). Confocal laser scanning microscopy analysis indicated that sub-MIC ciprofloxacin decreased biofilm formation, whereas tigecycline stimulated this process. Our data suggest that sub-MIC tigecycline may have bearing on the outcome of infections.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Biofilmes/crescimento & desenvolvimento
Ciprofloxacino/farmacologia
Regulação Bacteriana da Expressão Gênica/efeitos dos fármacos
Minociclina/análogos & derivados
Staphylococcus epidermidis/efeitos dos fármacos
Staphylococcus epidermidis/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/biossíntese
Proteínas de Bactérias/genética
Biofilmes/efeitos dos fármacos
Seres Humanos
Testes de Sensibilidade Microbiana
Microscopia Confocal
Minociclina/farmacologia
N-Acetil-Muramil-L-Alanina Amidase/biossíntese
N-Acetil-Muramil-L-Alanina Amidase/genética
RNA Mensageiro/genética
Fator sigma/biossíntese
Fator sigma/genética
Staphylococcus epidermidis/genética
Staphylococcus epidermidis/isolamento & purificação
Transferases/biossíntese
Transferases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (RNA, Messenger); 0 (SigB protein, Bacteria); 0 (Sigma Factor); 5E8K9I0O4U (Ciprofloxacin); 70JE2N95KR (tigecycline); EC 2.- (Transferases); EC 3.5.1.28 (N-Acetylmuramoyl-L-alanine Amidase); FYY3R43WGO (Minocycline)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE
[do] DOI:10.1099/mic.0.000453


  5 / 7046 MEDLINE  
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[PMID]:28418240
[Au] Autor:Dunbar KL; Scharf DH; Litomska A; Hertweck C
[Ad] Endereço:Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI) , Beutenbergstrasse 11a, 07745 Jena, Germany.
[Ti] Título:Enzymatic Carbon-Sulfur Bond Formation in Natural Product Biosynthesis.
[So] Source:Chem Rev;117(8):5521-5577, 2017 Apr 26.
[Is] ISSN:1520-6890
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sulfur plays a critical role for the development and maintenance of life on earth, which is reflected by the wealth of primary metabolites, macromolecules, and cofactors bearing this element. Whereas a large body of knowledge has existed for sulfur trafficking in primary metabolism, the secondary metabolism involving sulfur has long been neglected. Yet, diverse sulfur functionalities have a major impact on the biological activities of natural products. Recent research at the genetic, biochemical, and chemical levels has unearthed a broad range of enzymes, sulfur shuttles, and chemical mechanisms for generating carbon-sulfur bonds. This Review will give the first systematic overview on enzymes catalyzing the formation of organosulfur natural products.
[Mh] Termos MeSH primário: Produtos Biológicos/metabolismo
Carbono/metabolismo
Enxofre/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Hidrolases/metabolismo
Oxigenases/metabolismo
Transferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biological Products); 70FD1KFU70 (Sulfur); 7440-44-0 (Carbon); 8L70Q75FXE (Adenosine Triphosphate); EC 1.13.- (Oxygenases); EC 2.- (Transferases); EC 3.- (Hydrolases); EC 3.3.1.2 (adenosylmethionine hydrolase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170620
[Lr] Data última revisão:
170620
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170419
[St] Status:MEDLINE
[do] DOI:10.1021/acs.chemrev.6b00697


  6 / 7046 MEDLINE  
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[PMID]:28414460
[Au] Autor:Oudouhou F; Casu B; Dopgwa Puemi AS; Sygusch J; Baron C
[Ad] Endereço:Department of Biochemistry and Molecular Medicine, Faculty of Medicine, Université de Montréal , Montréal, QC, Canada.
[Ti] Título:Analysis of Novel Interactions between Components of the Selenocysteine Biosynthesis Pathway, SEPHS1, SEPHS2, SEPSECS, and SECp43.
[So] Source:Biochemistry;56(17):2261-2270, 2017 May 02.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In mammalian cells, the incorporation of the 21st amino acid, selenocysteine, into proteins is guided by the Sec machinery. The function of this protein complex requires several protein-protein and protein-RNA interactions, leading to the incorporation of selenocysteine at UGA codons. It is guided by stem-loop structures localized in the 3' untranslated regions of the selenoprotein-encoding genes. Here, we conducted a global analysis of interactions between the Sec biosynthesis and incorporation components using a bioluminescence resonance energy transfer assay in mammalian cells that showed that selenocysteine synthase (SEPSECS), SECp43, and selenophosphate synthetases SEPHS1 and SEPHS2 form oligomers in eukaryotic cells. We also showed that SEPHS2 interacts with SEPSECS and SEPHS1; these interactions were confirmed by co-immunoprecipitation. To further analyze the interactions of SECp43, the protein was expressed in Escherichia coli, and small-angle X-ray scattering analysis revealed that it is a globular protein comprising two RNA-binding domains. Using phage display, we identified potential interaction sites and highlighted two residues (K166 and P167) required for its dimerization. The SECp43 structural model presented here constitutes the basis of future exploration of the protein-protein interactions among early components of the selenocysteine biosynthesis and incorporation pathway.
[Mh] Termos MeSH primário: Aminoacil-tRNA Sintetases/metabolismo
Modelos Moleculares
Fosfotransferases/metabolismo
Proteínas de Ligação a RNA/metabolismo
Transferases/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Aminoacil-tRNA Sintetases/química
Aminoacil-tRNA Sintetases/genética
Técnicas de Transferência de Energia por Ressonância de Bioluminescência
Técnicas de Visualização da Superfície Celular
Reagentes para Ligações Cruzadas/farmacologia
Dimerização
Células HEK293
Seres Humanos
Imunoprecipitação
Mutação
Fosfotransferases/química
Fosfotransferases/genética
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/genética
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Espalhamento a Baixo Ângulo
Succinimidas/farmacologia
Transferases/química
Transferases/genética
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cross-Linking Reagents); 0 (RNA-Binding Proteins); 0 (Recombinant Fusion Proteins); 0 (SECp43 protein, human); 0 (Succinimides); EC 2.- (Transferases); EC 2.7.- (Phosphotransferases); EC 2.7.- (selenophosphate synthetase 2, human); EC 2.7.9.3 (SEPHS1 protein, human); EC 2.9.1.1 (selenium transferase); EC 6.1.1.- (Amino Acyl-tRNA Synthetases); EC 6.1.1.- (O-phosphoseryl-tRNA:selenocysteinyl-tRNA synthase, human); V9WYZ7QMDT (disuccinimidyl suberate)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170418
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b01116


  7 / 7046 MEDLINE  
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[PMID]:28321040
[Au] Autor:Ohnami S; Nagashima T; Urakami K; Shimoda Y; Kamada F; Saito J; Naruoka A; Serizawa M; Masuda Y; Ohnami S; Kusuhara M; Yamaguchi K
[Ad] Endereço:Cancer Diagnostics Research Division, Shizuoka Cancer Center Research Institute.
[Ti] Título:Whole exome sequencing detects variants of genes that mediate response to anticancer drugs.
[So] Source:J Toxicol Sci;42(2):137-144, 2017.
[Is] ISSN:1880-3989
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Certain interindividual differences affecting the efficacy of drug treatment and adverse drug reactions are caused by genetic variants, and their phenotypic effects differ among ethnic groups. In this study, we used whole exome sequencing (WES) systematically to identify germline mutations that influence the activities of drug-metabolizing enzymes, as well as that of a transporter. We analyzed DNA isolated from blood samples from 2,042 Japanese patients with diverse cancers. We identified sequence variants of CYP2B6 (rs3745274), CYP2C9 (rs1057910), CYP2C19 (rs4986893), CYP2C19 (rs4244285), TPMT (rs1142345), NAT2 (rs1799930), NAT2 (rs1799931), UGT1A1 (rs4148323), COMT (rs4680), ABCB1 (rs1045642), and CDA (rs60369023). Wider application of WES will help to determine the effects of mutations on the activities of proteins encoded by drug response genes, and the information gained will accelerate the development of personalized therapies for patients with cancer. Moreover, this knowledge may provide clues for preventing cancer before the onset of symptoms.
[Mh] Termos MeSH primário: Antineoplásicos/uso terapêutico
Neoplasias/tratamento farmacológico
Neoplasias/genética
[Mh] Termos MeSH secundário: Subfamília B de Transportador de Cassetes de Ligação de ATP/genética
Adulto
Idoso
Idoso de 80 Anos ou mais
Antineoplásicos/efeitos adversos
Grupo com Ancestrais do Continente Asiático/genética
Citidina Desaminase/genética
Sistema Enzimático do Citocromo P-450/genética
Exoma
Feminino
Regulação Neoplásica da Expressão Gênica
Variação Genética
Genótipo
Seres Humanos
Masculino
Meia-Idade
Mutação
Análise de Sequência de DNA
Transferases/genética
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCB1 protein, human); 0 (ATP Binding Cassette Transporter, Sub-Family B); 0 (Antineoplastic Agents); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 2.- (Transferases); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.2131/jts.42.137


  8 / 7046 MEDLINE  
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[PMID]:28223451
[Au] Autor:Zhang S; Burns-Huang KE; Janssen GV; Li H; Ovaa H; Hedstrom L; Darwin KH
[Ad] Endereço:Department of Microbiology, New York University School of Medicine, New York, New York, USA.
[Ti] Título: Proteasome Accessory Factor A (PafA) Can Transfer Prokaryotic Ubiquitin-Like Protein (Pup) between Substrates.
[So] Source:MBio;8(1), 2017 Feb 21.
[Is] ISSN:2150-7511
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The protein degradation machinery of includes a proteasome and a ubiquitin-like protein (Pup). Proteasome accessory factor A (PafA) attaches Pup to proteins to target them for degradation by the proteasome. Free Pup is unstable and never observed in extracts of , an observation that led us to hypothesize that PafA may need alternative sources of Pup. Here, we show that PafA can move Pup from one proteasome substrate, inositol 1-phosphate synthetase (Ino1), to two different proteins, malonyl coenzyme A (CoA)-acyl carrier protein transacylase (FabD) and lonely guy (Log). This apparent "transpupylation" reaction required a previously unrecognized depupylase activity in PafA, and, surprisingly, this depupylase activity was much more efficient than the activity of the dedicated depupylase Dop (deamidase of Pup). Thus, PafA can potentially use both newly synthesized Pup and recycled Pup to doom proteins for degradation. Unlike eukaryotes, which contain hundreds of ubiquitin ligases, Pup-containing bacteria appear to have a single ligase to pupylate dozens if not hundreds of different proteins. The observation that PafA can depupylate and transpupylate offers new insight into how protein stability is regulated in proteasome-bearing bacteria. Importantly, PafA and the dedicated depupylase Dop are each required for the full virulence of Thus, inhibition of both enzymes may be extremely attractive for the development of therapeutics against tuberculosis.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Mycobacterium tuberculosis/enzimologia
Mycobacterium tuberculosis/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
Transferases/metabolismo
Ubiquitinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Pup protein, Mycobacterium tuberculosis); 0 (Ubiquitins); EC 2.- (Transferases); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE


  9 / 7046 MEDLINE  
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[PMID]:28139350
[Au] Autor:Kudoh K; Hotta S; Sekine M; Fujii R; Uchida A; Kubota G; Kawano Y; Ihara M
[Ad] Endereço:Department of Bioscience and Food Production Science, Interdisciplinary Graduate School of Science and Technology, Shinshu University, 8304 Minamiminowa, Nagano 399-4511, Japan.
[Ti] Título:Overexpression of endogenous 1-deoxy-d-xylulose 5-phosphate synthase (DXS) in cyanobacterium Synechocystis sp. PCC6803 accelerates protein aggregation.
[So] Source:J Biosci Bioeng;123(5):590-596, 2017 May.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:1-Deoxy-d-xylulose 5-phosphate synthase (DXS) is a rate-limiting enzyme in the 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway, which is responsible for the production of precursors of all isoprenoids. In a previous study, we had examined the overexpression of an endogenous DXS in a Synechocystis sp. PCC6803 mutant (DXS_ox), and found that the dxs mRNA level was 4-fold higher than that in the wild-type (WT) strain. However, the DXS protein level was only 1.5-fold higher, leading to the assumption that the level might be regulated by post-transcriptional events. In this study, we have additionally introduced an exogenous isoprene synthase (IspS; which can release MEP pathway products from the cell as gaseous isoprene) into the WT and DXS_ox strains (WT-isP and DXSox-isP strains, respectively), and their detailed DXS expression profiles were investigated from the induction phase through to the late-logarithmic phase. In the induction phase, the isoprene productivity of the DXSox-isP strain was slightly but significantly (1.4- to 1.8-fold) higher than that of the WT-isP strain, whereas the levels were comparable in the other phases. Interestingly, the ratios of soluble:insoluble DXS protein were remarkably low in the DXSox-isP strain during the induction phase to the early-logarithmic phase, resulting in a moderate level of soluble DXS. All our results suggested that the high translation rate of DXS disturbs the refolding process of DXS. To enhance the concentration of the active DXS in cyanobacteria, the enhancement of the DXS maturation system or the introduction of exogenous and robust DXS proteins might be necessary.
[Mh] Termos MeSH primário: Agregados Proteicos
Synechocystis/genética
Synechocystis/metabolismo
Transferases/genética
Transferases/metabolismo
[Mh] Termos MeSH secundário: Alquil e Aril Transferases/biossíntese
Alquil e Aril Transferases/genética
Alquil e Aril Transferases/metabolismo
Butadienos
Eritritol/análogos & derivados
Eritritol/metabolismo
Gases/metabolismo
Hemiterpenos/biossíntese
Engenharia Metabólica
Pentanos
Pentosefosfatos/biossíntese
RNA Mensageiro/análise
Solubilidade
Fosfatos Açúcares/metabolismo
Terpenos/metabolismo
Transferases/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (1-deoxylulose 5-phosphate); 0 (2-C-methylerythritol 4-phosphate); 0 (Butadienes); 0 (Gases); 0 (Hemiterpenes); 0 (Pentanes); 0 (Pentosephosphates); 0 (Protein Aggregates); 0 (RNA, Messenger); 0 (Sugar Phosphates); 0 (Terpenes); 0A62964IBU (isoprene); EC 2.- (Transferases); EC 2.2.1.- (deoxyxylulose-5-phosphate synthase); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (isoprene synthase); RA96B954X6 (Erythritol)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE


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[PMID]:28130442
[Au] Autor:Li Z; Kitanishi K; Twahir UT; Cracan V; Chapman D; Warncke K; Banerjee R
[Ad] Endereço:From the Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0600 and.
[Ti] Título:Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B Enzyme IcmF.
[So] Source:J Biol Chem;292(10):3977-3987, 2017 Mar 10.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:IcmF is a 5'-deoxyadenosylcobalamin (AdoCbl)-dependent enzyme that catalyzes the carbon skeleton rearrangement of isobutyryl-CoA to butyryl-CoA. It is a bifunctional protein resulting from the fusion of a G-protein chaperone with GTPase activity and the cofactor- and substrate-binding mutase domains with isomerase activity. IcmF is prone to inactivation during catalytic turnover, thus setting up its dependence on a cofactor repair system. Herein, we demonstrate that the GTPase activity of IcmF powers the ejection of the inactive cob(II)alamin cofactor and requires the presence of an acceptor protein, adenosyltransferase, for receiving it. Adenosyltransferase in turn converts cob(II)alamin to AdoCbl in the presence of ATP and a reductant. The repaired cofactor is then reloaded onto IcmF in a GTPase-gated step. The mechanistic details of cofactor loading and offloading from the AdoCbl-dependent IcmF are distinct from those of the better characterized and homologous methylmalonyl-CoA mutase/G-protein chaperone system.
[Mh] Termos MeSH primário: Acil Coenzima A/metabolismo
Proteínas de Bactérias/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Proteínas de Ligação ao GTP/metabolismo
Metalochaperonas/metabolismo
Vitamina B 12/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Cristalografia por Raios X
Metilmalonil-CoA Mutase/metabolismo
Modelos Moleculares
Chaperonas Moleculares/metabolismo
Domínios Proteicos
Transferases/metabolismo
Vitamina B 12/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Bacterial Proteins); 0 (Metallochaperones); 0 (Molecular Chaperones); 15621-60-0 (isobutyryl-coenzyme A); 2140-48-9 (butyryl-coenzyme A); EC 2.- (Transferases); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (GTP-Binding Proteins); EC 5.4.99.2 (Methylmalonyl-CoA Mutase); P6YC3EG204 (Vitamin B 12)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170727
[Lr] Data última revisão:
170727
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170129
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.775957



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