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Pesquisa : D12.776.157.050 [Categoria DeCS]
Referências encontradas : 790 [refinar]
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[PMID]:28448715
[Au] Autor:Thiele GAR; Friedman CP; Tsai KJS; Beld J; Londergan CH; Charkoudian LK
[Ad] Endereço:Department of Chemistry, Haverford College , Haverford, Pennsylvania 19041-1392, United States.
[Ti] Título:Acyl Carrier Protein Cyanylation Delivers a Ketoacyl Synthase-Carrier Protein Cross-Link.
[So] Source:Biochemistry;56(20):2533-2536, 2017 05 23.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acyl carrier proteins (ACPs) are central hubs in polyketide and fatty acid biosynthetic pathways, but the fast motions of the ACP's phosphopantetheine (Ppant) arm make its conformational dynamics difficult to capture using traditional spectroscopic approaches. Here we report that converting the terminal thiol of Escherichia coli ACP's Ppant arm into a thiocyanate activates this site to form a selective cross-link with the active site cysteine of its partner ketoacyl synthase (FabF). The reaction releases a cyanide anion, which can be detected by infrared spectroscopy. This represents a practical and generalizable method for obtaining and visualizing ACP-protein complexes relevant to biocatalysis and will be valuable in future structural and engineering studies.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila/química
Cianetos/química
Policetídeo Sintases/química
[Mh] Termos MeSH secundário: Cromatografia em Gel
Proteínas de Escherichia coli/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Cyanides); 0 (Escherichia coli Proteins); 79956-01-7 (Polyketide Synthases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171205
[Lr] Data última revisão:
171205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00219


  2 / 790 MEDLINE  
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[PMID]:28961247
[Au] Autor:Ke X; Zou W; Ren Y; Wang Z; Li J; Wu X; Zhao J
[Ad] Endereço:State Key Laboratory of Hybrid Rice, College of Life Sciences, Wuhan University, Wuhan, China.
[Ti] Título:Functional divergence of chloroplast Cpn60α subunits during Arabidopsis embryo development.
[So] Source:PLoS Genet;13(9):e1007036, 2017 Sep.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chaperonins are a class of molecular chaperones that assist in the folding and assembly of a wide range of substrates. In plants, chloroplast chaperonins are composed of two different types of subunits, Cpn60α and Cpn60ß, and duplication of Cpn60α and Cpn60ß genes occurs in a high proportion of plants. However, the importance of multiple Cpn60α and Cpn60ß genes in plants is poorly understood. In this study, we found that loss-of-function of CPNA2 (AtCpn60α2), a gene encoding the minor Cpn60α subunit in Arabidopsis thaliana, resulted in arrested embryo development at the globular stage, whereas the other AtCpn60α gene encoding the dominant Cpn60α subunit, CPNA1 (AtCpn60α1), mainly affected embryonic cotyledon development at the torpedo stage and thereafter. Further studies demonstrated that CPNA2 can form a functional chaperonin with CPNB2 (AtCpn60ß2) and CPNB3 (AtCpn60ß3), while the functional partners of CPNA1 are CPNB1 (AtCpn60ß1) and CPNB2. We also revealed that the functional chaperonin containing CPNA2 could assist the folding of a specific substrate, KASI (ß-ketoacyl-[acyl carrier protein] synthase I), and that the KASI protein level was remarkably reduced due to loss-of-function of CPNA2. Furthermore, the reduction in the KASI protein level was shown to be the possible cause for the arrest of cpna2 embryos. Our findings indicate that the two Cpn60α subunits in Arabidopsis play different roles during embryo development through forming distinct chaperonins with specific AtCpn60ß to assist the folding of particular substrates, thus providing novel insights into functional divergence of Cpn60α subunits in plants.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/genética
Chaperoninas/metabolismo
Regulação da Expressão Gênica de Plantas
Genes de Plantas
[Mh] Termos MeSH secundário: 3-Oxoacil-(Proteína de Transporte de Acila) Sintase/genética
3-Oxoacil-(Proteína de Transporte de Acila) Sintase/metabolismo
Proteína de Transporte de Acila/genética
Proteína de Transporte de Acila/metabolismo
Sequência de Aminoácidos
Arabidopsis/embriologia
Arabidopsis/crescimento & desenvolvimento
Proteínas de Arabidopsis/genética
Chaperoninas/genética
Cloroplastos/genética
Cloroplastos/metabolismo
Clonagem Molecular
Cotilédone/embriologia
Cotilédone/genética
Duplicação Gênica
Conformação Proteica
Plântulas/embriologia
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Arabidopsis Proteins); EC 2.3.1.41 (3-Oxoacyl-(Acyl-Carrier-Protein) Synthase); EC 3.6.1.- (Chaperonins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170930
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007036


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[PMID]:28615445
[Au] Autor:Braymer JJ; Lill R
[Ad] Endereço:From the Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg and.
[Ti] Título:Iron-sulfur cluster biogenesis and trafficking in mitochondria.
[So] Source:J Biol Chem;292(31):12754-12763, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes is a multistage, multicompartment process that is essential for a broad range of cellular functions, including genome maintenance, protein translation, energy conversion, and the antiviral response. Genetic and cell biological studies over almost 2 decades have revealed some 30 proteins involved in the synthesis of cellular [2Fe-2S] and [4Fe-4S] clusters and their incorporation into numerous apoproteins. Mechanistic aspects of Fe/S protein biogenesis continue to be elucidated by biochemical and ultrastructural investigations. Here, we review recent developments in the pursuit of constructing a comprehensive model of Fe/S protein assembly in the mitochondrion.
[Mh] Termos MeSH primário: Regulação Enzimológica da Expressão Gênica
Proteínas com Ferro-Enxofre/metabolismo
Mitocôndrias/metabolismo
Modelos Biológicos
Modelos Moleculares
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila/química
Proteína de Transporte de Acila/genética
Proteína de Transporte de Acila/metabolismo
Adrenodoxina/química
Adrenodoxina/genética
Adrenodoxina/metabolismo
Animais
Apoenzimas/química
Apoenzimas/genética
Apoenzimas/metabolismo
Seres Humanos
Proteínas de Ligação ao Ferro/química
Proteínas de Ligação ao Ferro/genética
Proteínas de Ligação ao Ferro/metabolismo
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/genética
Mitocôndrias/enzimologia
Proteínas Mitocondriais/química
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Conformação Proteica
Dobramento de Proteína
Multimerização Proteica
Transporte Proteico
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Especificidade da Espécie
Sulfurtransferases/química
Sulfurtransferases/genética
Sulfurtransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Apoenzymes); 0 (ISU1 protein, S cerevisiae); 0 (Iron-Binding Proteins); 0 (Iron-Sulfur Proteins); 0 (Isd11 protein, S cerevisiae); 0 (Mitochondrial Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (YAH1 protein, S cerevisiae); 0 (frataxin); 12687-22-8 (Adrenodoxin); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.7 (NFS1 protein, S cerevisiae)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R117.787101


  4 / 790 MEDLINE  
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[PMID]:28233492
[Au] Autor:Cai K; Frederick RO; Tonelli M; Markley JL
[Ad] Endereço:Biochemistry Department, University of Wisconsin-Madison , 433 Babcock Drive, Madison, Wisconsin 53706, United States.
[Ti] Título:Mitochondrial Cysteine Desulfurase and ISD11 Coexpressed in Escherichia coli Yield Complex Containing Acyl Carrier Protein.
[So] Source:ACS Chem Biol;12(4):918-921, 2017 Apr 21.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial cysteine desulfurase is an essential component of the machinery for iron-sulfur cluster biosynthesis. It has been known that human cysteine desulfurase that is catalytically active in vitro can be prepared by overexpressing in Escherichia coli cells two protein components of this system, the cysteine desulfurase protein NFS1 and the auxiliary protein ISD11. We report here that this active preparation contains, in addition, the holo-form of E. coli acyl carrier protein (Acp). We have determined the stoichiometry of the complex to be [Acp] :[ISD11] :[NFS1] . Acyl carrier protein recently has been found to be an essential component of the iron-sulfur protein biosynthesis machinery in mitochondria; thus, because of the activity of [Acp] :[ISD11] :[NFS1] in supporting iron-sulfur cluster assembly in vitro, it appears that E. coli Acp can substitute for its human homologue.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila/metabolismo
Liases de Carbono-Enxofre/metabolismo
Escherichia coli/genética
Proteínas Reguladoras do Ferro/metabolismo
Mitocôndrias/enzimologia
[Mh] Termos MeSH secundário: Liases de Carbono-Enxofre/genética
Cromatografia em Gel
Eletroforese em Gel de Poliacrilamida
Proteínas Reguladoras do Ferro/genética
Mitocôndrias/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Espalhamento a Baixo Ângulo
Espectrometria de Massas em Tandem
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (ISD11 protein, human); 0 (Iron-Regulatory Proteins); 0 (Recombinant Proteins); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (cysteine desulfurase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.6b01005


  5 / 790 MEDLINE  
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[PMID]:28218529
[Au] Autor:Iorio M; Cruz J; Simone M; Bernasconi A; Brunati C; Sosio M; Donadio S; Maffioli SI
[Ad] Endereço:Naicons Srl , Viale Ortles 22/4, 20139 Milano, Italy.
[Ti] Título:Antibacterial Paramagnetic Quinones from Actinoallomurus.
[So] Source:J Nat Prod;80(4):819-827, 2017 Apr 28.
[Is] ISSN:1520-6025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Four metabolites, designated paramagnetoquinone A, B, C, and D (1-4), were isolated from three strains belonging to the actinomycete genus Actinoallomurus. Compounds 1 and 2 showed potent antibacterial activity with MIC values lower than 0.015 µg/mL against Gram-positive pathogens, including antibiotic-resistant strains. Since compounds 1 and 2 were NMR-silent due to the presence of an oxygen radical, structure elucidation was achieved through a combination of derivatizations, oxidations, and analysis of C-labeled compounds. The paramagnetoquinones share the same carbon scaffold as tetracenomycin but carry two quinones and a five-membered lactone fused to the aromatic system. Compounds 2 and 1 are identical except for an unprecedented replacement of a methoxy in 2 by a methylamino group in 1. Related compounds devoid of methyl group(s) and of antibacterial activity were isolated from a different Actinoallomurus strain. The likely pmq biosynthetic gene cluster was identified from strain ID145113. While the cluster encodes many of the expected enzymes involved in the formation of aromatic polyketides, it also encodes a dedicated ketoacid dehydrogenase complex and an unusual acyl carrier protein transacylase, suggesting that an unusual starter unit might prime the polyketide synthase.
[Mh] Termos MeSH primário: Actinomycetales/química
Antibacterianos/isolamento & purificação
Antibacterianos/farmacologia
Quinonas/isolamento & purificação
Quinonas/farmacologia
[Mh] Termos MeSH secundário: Actinomycetales/genética
Proteína de Transporte de Acila/metabolismo
Antibacterianos/química
Testes de Sensibilidade Microbiana
Estrutura Molecular
Filogenia
Policetídeo Sintases/metabolismo
Policetídeos
Quinonas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Anti-Bacterial Agents); 0 (Polyketides); 0 (Quinones); 0 (paramagnetoquinone A); 79956-01-7 (Polyketide Synthases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jnatprod.6b00654


  6 / 790 MEDLINE  
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[PMID]:28196402
[Au] Autor:Manandhar M; Cronan JE
[Ad] Endereço:Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.
[Ti] Título:Pimelic acid, the first precursor of the Bacillus subtilis biotin synthesis pathway, exists as the free acid and is assembled by fatty acid synthesis.
[So] Source:Mol Microbiol;104(4):595-607, 2017 05.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Biotin synthetic pathways are readily separated into two stages, synthesis of the seven carbon α, ω-dicarboxylic acid pimelate moiety and assembly of the fused heterocyclic rings. The biotin pathway genes responsible for pimelate moiety synthesis vary widely among bacteria whereas the ring synthesis genes are highly conserved. Bacillus subtilis seems to have redundant genes, bioI and bioW, for generation of the pimelate intermediate. Largely consistent with previous genetic studies it was found that deletion of bioW caused a biotin auxotrophic phenotype whereas deletion of bioI did not. BioW is a pimeloyl-CoA synthetase that converts pimelic acid to pimeloyl-CoA. The essentiality of BioW for biotin synthesis indicates that the free form of pimelic acid is an intermediate in biotin synthesis although this is not the case in E. coli. Since the origin of pimelic acid in Bacillus subtilis is unknown, C-NMR studies were carried out to decipher the pathway for its generation. The data provided evidence for the role of free pimelate in biotin synthesis and the involvement of fatty acid synthesis in pimelate production. Cerulenin, an inhibitor of the key fatty acid elongation enzyme, FabF, markedly decreased biotin production by B. subtilis resting cells whereas a strain having a cerulenin-resistant FabF mutant produced more biotin. In addition, supplementation with pimelic acid fully restored biotin production in cerulenin-treated cells. These results indicate that pimelic acid originating from fatty acid synthesis pathway is a bona fide precursor of biotin in B. subtilis.
[Mh] Termos MeSH primário: Biotina/biossíntese
Ácidos Pimélicos/metabolismo
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila/metabolismo
Acil Coenzima A/genética
Acil Coenzima A/metabolismo
Bacillus subtilis/genética
Bacillus subtilis/metabolismo
Vias Biossintéticas
Biotina/metabolismo
Clonagem Molecular
Coenzima A Ligases/genética
Coenzima A Ligases/metabolismo
Ácidos Graxos/metabolismo
Ácidos Pimélicos/química
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Acyl Coenzyme A); 0 (Fatty Acids); 0 (Pimelic Acids); 18907-20-5 (pimeloyl-coenzyme A); 6SO6U10H04 (Biotin); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.- (pimeloyl-CoA synthetase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170215
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13648


  7 / 790 MEDLINE  
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[PMID]:28187530
[Au] Autor:Paul S; Ishida H; Nguyen LT; Liu Z; Vogel HJ
[Ad] Endereço:Biochemistry Research Group, Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada.
[Ti] Título:Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics.
[So] Source:Protein Sci;26(5):946-959, 2017 May.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Friulimicin is a cyclic lipodecapeptide antibiotic that is produced by Actinoplanes friuliensis. Similar to the related lipopeptide drug daptomycin, the peptide skeleton of friulimicin is synthesized by a large multienzyme nonribosomal peptide synthetase (NRPS) system. The LipD protein plays a major role in the acylation reaction of friulimicin. The attachment of the fatty acid group promotes its antibiotic activity. Phylogenetic analysis reveals that LipD is most closely related to other freestanding acyl carrier proteins (ACPs), for which the genes are located near to NRPS gene clusters. Here, we report that the solution NMR structure of apo-LipD is very similar to other four-helix bundle forming ACPs from fatty acid synthase (FAS), polyketide synthase, and NRPS systems. By recording NMR dynamics data, we found that the backbone motions in holo-LipD are more restricted than in apo-LipD due to the attachment of phosphopantetheine moiety. This enhanced stability of holo-LipD was also observed in differential scanning calorimetry experiments. Furthermore, we demonstrate that, unlike several other ACPs, the folding of LipD does not depend on the presence of divalent cations, although the presence of Mg or Ca can increase the protein stability. We propose that small structural rearrangements in the tertiary structure of holo-LipD which lead to the enhanced stability are important for the cognate enzyme recognition for the acylation reaction. Our results also highlight the different surface charges of LipD and FAS-ACP from A. friuliensis that would allow the acyl-CoA ligase to interact preferentially with the LipD instead of binding to the FAS-ACP.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila/química
Antibacterianos/biossíntese
Proteínas de Bactérias/química
Lipopeptídeos/biossíntese
Micromonosporaceae/química
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila/metabolismo
Proteínas de Bactérias/metabolismo
Espectroscopia de Ressonância Magnética
Micromonosporaceae/metabolismo
Peptídeo Sintases/química
Peptídeo Sintases/metabolismo
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Lipopeptides); EC 6.3.2.- (Peptide Synthases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170211
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3138


  8 / 790 MEDLINE  
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[PMID]:28085879
[Au] Autor:Viala JP; Prima V; Puppo R; Agrebi R; Canestrari MJ; Lignon S; Chauvin N; Méresse S; Mignot T; Lebrun R; Bouveret E
[Ad] Endereço:Aix Marseille Univ, CNRS, IMM, LISM, Marseille, France.
[Ti] Título:Acylation of the Type 3 Secretion System Translocon Using a Dedicated Acyl Carrier Protein.
[So] Source:PLoS Genet;13(1):e1006556, 2017 Jan.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacterial pathogens often deliver effectors into host cells using type 3 secretion systems (T3SS), the extremity of which forms a translocon that perforates the host plasma membrane. The T3SS encoded by Salmonella pathogenicity island 1 (SPI-1) is genetically associated with an acyl carrier protein, IacP, whose role has remained enigmatic. In this study, using tandem affinity purification, we identify a direct protein-protein interaction between IacP and the translocon protein SipB. We show, by mass spectrometry and radiolabelling, that SipB is acylated, which provides evidence for a modification of the translocon that has not been described before. A unique and conserved cysteine residue of SipB is identified as crucial for this modification. Although acylation of SipB was not essential to virulence, we show that this posttranslational modification promoted SipB insertion into host-cell membranes and pore-forming activity linked to the SPI-1 T3SS. Cooccurrence of acyl carrier and translocon proteins in several γ- and ß-proteobacteria suggests that acylation of the translocon is conserved in these other pathogenic bacteria. These results also indicate that acyl carrier proteins, known for their involvement in metabolic pathways, have also evolved as cofactors of new bacterial protein lipidation pathways.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila/metabolismo
Sistemas de Secreção Tipo III/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Proteína de Transporte de Acila/genética
Proteínas de Bactérias/metabolismo
Proteínas de Membrana/metabolismo
Processamento de Proteína Pós-Traducional
Salmonella typhimurium/genética
Salmonella typhimurium/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Bacterial Proteins); 0 (Membrane Proteins); 0 (Type III Secretion Systems); 0 (invasion protein B, Salmonella typhimurium)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170524
[Lr] Data última revisão:
170524
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170114
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006556


  9 / 790 MEDLINE  
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[PMID]:28001042
[Au] Autor:Cai K; Tonelli M; Frederick RO; Markley JL
[Ad] Endereço:Mitochondrial Protein Partnership, Center for Eukaryotic Structural Genomics, and ‡National Magnetic Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
[Ti] Título:Human Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron-Sulfur Cluster Biosynthesis.
[So] Source:Biochemistry;56(3):487-499, 2017 Jan 24.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ferredoxins play an important role as an electron donor in iron-sulfur (Fe-S) cluster biosynthesis. Two ferredoxins, human mitochondrial ferredoxin 1 (FDX1) and human mitochondrial ferredoxin 2 (FDX2), are present in the matrix of human mitochondria. Conflicting results have been reported regarding their respective function in mitochondrial iron-sulfur cluster biogenesis. We report here biophysical studies of the interaction of these two ferredoxins with other proteins involved in mitochondrial iron-sulfur cluster assembly. Results from nuclear magnetic resonance spectroscopy show that both FDX1 and FDX2 (in both their reduced and oxidized states) interact with the protein complex responsible for cluster assembly, which contains cysteine desulfurase (NFS1), ISD11 (also known as LYRM4), and acyl carrier protein (Acp). In all cases, ferredoxin residues close to the Fe-S cluster are involved in the interaction with this complex. Isothermal titration calorimetry results showed that FDX2 binds more tightly to the cysteine desulfurase complex than FDX1 does. The reduced form of each ferredoxin became oxidized in the presence of the cysteine desulfurase complex when l-cysteine was added, leading to its conversion to l-alanine and the generation of sulfide. In an in vitro reaction, the reduced form of each ferredoxin was found to support Fe-S cluster assembly on ISCU; the rate of cluster assembly was faster with FDX2 than with FDX1. Taken together, these results show that both FDX1 and FDX2 can function in Fe-S cluster assembly in vitro.
[Mh] Termos MeSH primário: Liases de Carbono-Enxofre/química
Ferredoxinas/química
Ferro/química
Enxofre/química
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila/genética
Proteína de Transporte de Acila/metabolismo
Sequência de Aminoácidos
Animais
Liases de Carbono-Enxofre/genética
Liases de Carbono-Enxofre/metabolismo
Cisteína
Elétrons
Escherichia coli/genética
Escherichia coli/metabolismo
Ferredoxinas/genética
Ferredoxinas/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Ferro/metabolismo
Proteínas de Ligação ao Ferro/genética
Proteínas de Ligação ao Ferro/metabolismo
Proteínas Reguladoras do Ferro/genética
Proteínas Reguladoras do Ferro/metabolismo
Proteínas com Ferro-Enxofre/genética
Proteínas com Ferro-Enxofre/metabolismo
Mitocôndrias/genética
Mitocôndrias/metabolismo
Modelos Moleculares
Oxirredução
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Alinhamento de Sequência
Enxofre/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Ferredoxins); 0 (ISCU protein, human); 0 (ISD11 protein, human); 0 (Iron-Binding Proteins); 0 (Iron-Regulatory Proteins); 0 (Iron-Sulfur Proteins); 0 (Recombinant Proteins); 0 (frataxin); 70FD1KFU70 (Sulfur); E1UOL152H7 (Iron); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (NFS1 protein, human); K848JZ4886 (Cysteine)
[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:161222
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00447


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Fotocópia
[PMID]:27986898
[Au] Autor:Otsuka T; Brauer AL; Kirkham C; Sully EK; Pettigrew MM; Kong Y; Geller BL; Murphy TF
[Ad] Endereço:Division of Infectious Diseases, Department of Medicine, University at Buffalo, State University of New York, Buffalo, NY, USA.
[Ti] Título:Antimicrobial activity of antisense peptide-peptide nucleic acid conjugates against non-typeable Haemophilus influenzae in planktonic and biofilm forms.
[So] Source:J Antimicrob Chemother;72(1):137-144, 2017 Jan.
[Is] ISSN:1460-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Antisense peptide nucleic acids (PNAs) are synthetic polymers that mimic DNA/RNA and inhibit bacterial gene expression in a sequence-specific manner. METHODS: To assess activity against non-typeable Haemophilus influenzae (NTHi), we designed six PNA-peptides that target acpP, encoding an acyl carrier protein. MICs and minimum biofilm eradication concentrations (MBECs) were determined. Resistant strains were selected by serial passages on media with a sub-MIC concentration of acpP-PNA. RESULTS: The MICs of six acpP-PNA-peptides were 2.9-11 mg/L (0.63-2.5 µmol/L) for 20 clinical isolates, indicating susceptibility of planktonic NTHi. By contrast, MBECs were up to 179 mg/L (40 µmol/L). Compared with one original PNA-peptide (acpP-PNA1-3'N), an optimized PNA-peptide (acpP-PNA14-5'L) differs in PNA sequence and has a 5' membrane-penetrating peptide with a linker between the PNA and peptide. The optimized PNA-peptide had an MBEC ranging from 11 to 23 mg/L (2.5-5 µmol/L), indicating susceptibility. A resistant strain that was selected by the original acpP-PNA1-3'N had an SNP that introduced a stop codon in NTHI0044, which is predicted to encode an ATP-binding protein of a conserved ABC transporter. Deletion of NTHI0044 caused resistance to the original acpP-PNA1-3'N, but showed no effect on susceptibility to the optimized acpP-PNA14-5'L. The WT strain remained susceptible to the optimized PNA-peptide after 30 serial passages on media containing the optimized PNA-peptide. CONCLUSIONS: A PNA-peptide that targets acpP, has a 5' membrane-penetrating peptide and has a linker shows excellent activity against planktonic and biofilm NTHi and is associated with a low risk for induction of resistance.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila/antagonistas & inibidores
Antibacterianos/farmacologia
Biofilmes/efeitos dos fármacos
Haemophilus influenzae/efeitos dos fármacos
Oligodesoxirribonucleotídeos Antissenso/farmacologia
Ácidos Nucleicos Peptídicos/farmacologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/antagonistas & inibidores
Farmacorresistência Bacteriana
Haemophilus influenzae/fisiologia
Testes de Sensibilidade Microbiana
Inoculações Seriadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Oligodeoxyribonucleotides, Antisense); 0 (Peptide Nucleic Acids)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161218
[St] Status:MEDLINE



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