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[PMID]:29176894
[Au] Autor:Levillain F; Poquet Y; Mallet L; Mazères S; Marceau M; Brosch R; Bange FC; Supply P; Magalon A; Neyrolles O
[Ad] Endereço:Institut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, Toulouse, France.
[Ti] Título:Horizontal acquisition of a hypoxia-responsive molybdenum cofactor biosynthesis pathway contributed to Mycobacterium tuberculosis pathoadaptation.
[So] Source:PLoS Pathog;13(11):e1006752, 2017 Nov.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The unique ability of the tuberculosis (TB) bacillus, Mycobacterium tuberculosis, to persist for long periods of time in lung hypoxic lesions chiefly contributes to the global burden of latent TB. We and others previously reported that the M. tuberculosis ancestor underwent massive episodes of horizontal gene transfer (HGT), mostly from environmental species. Here, we sought to explore whether such ancient HGT played a part in M. tuberculosis evolution towards pathogenicity. We were interested by a HGT-acquired M. tuberculosis-specific gene set, namely moaA1-D1, which is involved in the biosynthesis of the molybdenum cofactor. Horizontal acquisition of this gene set was striking because homologues of these moa genes are present all across the Mycobacterium genus, including in M. tuberculosis. Here, we discovered that, unlike their paralogues, the moaA1-D1 genes are strongly induced under hypoxia. In vitro, a M. tuberculosis moaA1-D1-null mutant has an impaired ability to respire nitrate, to enter dormancy and to survive in oxygen-limiting conditions. Conversely, heterologous expression of moaA1-D1 in the phylogenetically closest non-TB mycobacterium, Mycobacterium kansasii, which lacks these genes, improves its capacity to respire nitrate and grants it with a marked ability to survive oxygen depletion. In vivo, the M. tuberculosis moaA1-D1-null mutant shows impaired survival in hypoxic granulomas in C3HeB/FeJ mice, but not in normoxic lesions in C57BL/6 animals. Collectively, our results identify a novel pathway required for M. tuberculosis resistance to host-imposed stress, namely hypoxia, and provide evidence that ancient HGT bolstered M. tuberculosis evolution from an environmental species towards a pervasive human-adapted pathogen.
[Mh] Termos MeSH primário: Coenzimas/biossíntese
Transferência Genética Horizontal
Metaloproteínas/biossíntese
Mycobacterium tuberculosis/genética
Mycobacterium tuberculosis/metabolismo
Oxigênio/metabolismo
Tuberculose/microbiologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Feminino
Regulação Bacteriana da Expressão Gênica
Seres Humanos
Hipóxia/metabolismo
Hipóxia/microbiologia
Camundongos
Camundongos Endogâmicos C57BL
Mycobacterium/genética
Mycobacterium/metabolismo
Nitratos/metabolismo
Pteridinas
Tuberculose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Metalloproteins); 0 (Nitrates); 0 (Pteridines); 73508-07-3 (molybdenum cofactor); S88TT14065 (Oxygen)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180109
[Lr] Data última revisão:
180109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006752


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[PMID]:28941802
[Au] Autor:Valdivieso ÁG; Mori C; Clauzure M; Massip-Copiz M; Santa-Coloma TA
[Ad] Endereço:Institute for Biomedical Research (BIOMED, UCA-CONICET), Laboratory of Cellular and Molecular Biology, School of Medical Sciences, Pontifical Catholic University of Argentina (UCA) and The National Scientific and Technical Research Council of Argentina (CONICET), Buenos Aires, C1107AFF, Argentina.
[Ti] Título:CFTR modulates RPS27 gene expression using chloride anion as signaling effector.
[So] Source:Arch Biochem Biophys;633:103-109, 2017 Nov 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In Cystic Fibrosis (CF), the impairment of the CFTR channel activity leads to a variety of alterations, including differential gene expression. However, the CFTR signaling mechanisms remain unclear. Recently, culturing IB3-1 CF cells under different intracellular Cl concentrations ([Cl ] ), we observed several Cl -dependent genes and further characterized one of them as RPS27. Thus, we hypothesized that Cl might act as a signaling effector for CFTR signaling. Here, to test this idea, we study RPS27 expression in T84 cells modulating the CFTR activity by using CFTR inhibitors. First, we observed that incubation of T84 cells with increasing concentrations of the CFTR inhibitors CFTR(inh)-172 or GlyH-101 determined a progressive increase in the relative [Cl ] (using the Cl fluorescent probe SPQ). The [Cl ] rise was concomitant with a dose-dependent down-regulation of RPS27. These results imply that CFTR inhibition produce Cl accumulation and that RPS27 expression can be modulated by CFTR inhibition. Therefore, Cl behaves as a signaling effector for CFTR in the modulation of RPS27 expression. In addition, the IL-1ß receptor antagonist IL1RN or the JNK inhibitor SP600125, both restored the down-regulation of RPS27 induced by CFTRinh-172, implying a role of autocrine IL-1ß and JNK signaling downstream of Cl in RPS27 modulation.
[Mh] Termos MeSH primário: Cloretos/metabolismo
Regulador de Condutância Transmembrana em Fibrose Cística/genética
Células Epiteliais/metabolismo
Metaloproteínas/genética
Proteínas Nucleares/genética
Proteínas de Ligação a RNA/genética
Proteínas Ribossômicas/genética
Transdução de Sinais
[Mh] Termos MeSH secundário: Antracenos/farmacologia
Comunicação Autócrina
Benzoatos/farmacologia
Linhagem Celular Tumoral
Regulador de Condutância Transmembrana em Fibrose Cística/antagonistas & inibidores
Regulador de Condutância Transmembrana em Fibrose Cística/metabolismo
Células Epiteliais/citologia
Células Epiteliais/efeitos dos fármacos
Corantes Fluorescentes/metabolismo
Regulação da Expressão Gênica
Glicina/análogos & derivados
Glicina/farmacologia
Seres Humanos
Hidrazinas/farmacologia
Proteína Antagonista do Receptor de Interleucina 1/farmacologia
Interleucina-1beta/antagonistas & inibidores
Interleucina-1beta/genética
Interleucina-1beta/metabolismo
Transporte de Íons/efeitos dos fármacos
MAP Quinase Quinase 4/antagonistas & inibidores
MAP Quinase Quinase 4/genética
MAP Quinase Quinase 4/metabolismo
Metaloproteínas/metabolismo
Proteínas Nucleares/metabolismo
Inibidores de Proteínas Quinases/farmacologia
Proteínas de Ligação a RNA/metabolismo
Proteínas Ribossômicas/metabolismo
Tiazolidinas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3-((3-trifluoromethyl)phenyl)-5-((3-carboxyphenyl)methylene)-2-thioxo-4-thiazolidinone); 0 (Anthracenes); 0 (Benzoates); 0 (CFTR protein, human); 0 (Chlorides); 0 (Fluorescent Dyes); 0 (Hydrazines); 0 (IL1B protein, human); 0 (IL1RN protein, human); 0 (Interleukin 1 Receptor Antagonist Protein); 0 (Interleukin-1beta); 0 (Metalloproteins); 0 (N-(2-naphthalenyl)-((3,5-dibromo-2,4-dihydroxyphenyl)methylene)glycine hydrazide); 0 (Nuclear Proteins); 0 (Protein Kinase Inhibitors); 0 (RNA-Binding Proteins); 0 (RPS27 protein, human); 0 (Ribosomal Proteins); 0 (Thiazolidines); 126880-72-6 (Cystic Fibrosis Transmembrane Conductance Regulator); 1TW30Y2766 (pyrazolanthrone); EC 2.7.12.2 (MAP Kinase Kinase 4); TE7660XO1C (Glycine)
[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:170925
[St] Status:MEDLINE


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[PMID]:28887302
[Au] Autor:Neupane DP; Avalos D; Fullam S; Roychowdhury H; Yukl ET
[Ad] Endereço:From the Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003.
[Ti] Título:Mechanisms of zinc binding to the solute-binding protein AztC and transfer from the metallochaperone AztD.
[So] Source:J Biol Chem;292(42):17496-17505, 2017 Oct 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacteria can acquire the essential metal zinc from extremely zinc-limited environments by using ATP-binding cassette (ABC) transporters. These transporters are critical virulence factors, relying on specific and high-affinity binding of zinc by a periplasmic solute-binding protein (SBP). As such, the mechanisms of zinc binding and release among bacterial SBPs are of considerable interest as antibacterial drug targets. Zinc SBPs are characterized by a flexible loop near the high-affinity zinc-binding site. The function of this structure is not always clear, and its flexibility has thus far prevented structural characterization by X-ray crystallography. Here, we present intact structures for the zinc-specific SBP AztC from the bacterium in the zinc-bound and apo-states. A comparison of these structures revealed that zinc loss prompts significant structural rearrangements, mediated by the formation of a sodium-binding site in the apo-structure. We further show that the AztC flexible loop has no impact on zinc-binding affinity, stoichiometry, or protein structure, yet is essential for zinc transfer from the metallochaperone AztD. We also found that 3 His residues in the loop appear to temporarily coordinate zinc and then convey it to the high-affinity binding site. Thus, mutation of any of these residues to Ala abrogated zinc transfer from AztD. Our structural and mechanistic findings conclusively identify a role for the AztC flexible loop in zinc acquisition from the metallochaperone AztD, yielding critical insights into metal binding by AztC from both solution and AztD. These proteins are highly conserved in human pathogens, making this work potentially useful for the development of novel antibiotics.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Metaloproteínas/química
Chaperonas Moleculares/química
Paracoccus denitrificans/química
Zinco/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Cristalografia por Raios X
Metaloproteínas/genética
Metaloproteínas/metabolismo
Chaperonas Moleculares/genética
Chaperonas Moleculares/metabolismo
Paracoccus denitrificans/genética
Paracoccus denitrificans/metabolismo
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Metalloproteins); 0 (Molecular Chaperones); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171028
[Lr] Data última revisão:
171028
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170910
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.804799


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[PMID]:28766335
[Au] Autor:Bühning M; Friemel M; Leimkühler S
[Ad] Endereço:Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam , D-14476 Potsdam, Germany.
[Ti] Título:Functional Complementation Studies Reveal Different Interaction Partners of Escherichia coli IscS and Human NFS1.
[So] Source:Biochemistry;56(34):4592-4605, 2017 Aug 29.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The trafficking and delivery of sulfur to cofactors and nucleosides is a highly regulated and conserved process among all organisms. All sulfur transfer pathways generally have an l-cysteine desulfurase as an initial sulfur-mobilizing enzyme in common, which serves as a sulfur donor for the biosynthesis of sulfur-containing biomolecules like iron-sulfur (Fe-S) clusters, thiamine, biotin, lipoic acid, the molybdenum cofactor (Moco), and thiolated nucleosides in tRNA. The human l-cysteine desulfurase NFS1 and the Escherichia coli homologue IscS share a level of amino acid sequence identity of ∼60%. While E. coli IscS has a versatile role in the cell and was shown to have numerous interaction partners, NFS1 is mainly localized in mitochondria with a crucial role in the biosynthesis of Fe-S clusters. Additionally, NFS1 is also located in smaller amounts in the cytosol with a role in Moco biosynthesis and mcm s U34 thio modifications of nucleosides in tRNA. NFS1 and IscS were conclusively shown to have different interaction partners in their respective organisms. Here, we used functional complementation studies of an E. coli iscS deletion strain with human NFS1 to dissect their conserved roles in the transfer of sulfur to a specific target protein. Our results show that human NFS1 and E. coli IscS share conserved binding sites for proteins involved in Fe-S cluster assembly like IscU, but not with proteins for tRNA thio modifications or Moco biosynthesis. In addition, we show that human NFS1 was almost fully able to complement the role of IscS in Moco biosynthesis when its specific interaction partner protein MOCS3 from humans was also present.
[Mh] Termos MeSH primário: Liases de Carbono-Enxofre
Coenzimas
Escherichia coli
Teste de Complementação Genética
Metaloproteínas
Pteridinas
[Mh] Termos MeSH secundário: Sítios de Ligação
Liases de Carbono-Enxofre/genética
Liases de Carbono-Enxofre/metabolismo
Coenzimas/biossíntese
Coenzimas/genética
Escherichia coli/enzimologia
Escherichia coli/genética
Seres Humanos
Metaloproteínas/biossíntese
Metaloproteínas/genética
Nucleotidiltransferases/metabolismo
RNA Bacteriano/genética
RNA Bacteriano/metabolismo
RNA de Transferência/metabolismo
Sulfurtransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 0 (Metalloproteins); 0 (Pteridines); 0 (RNA, Bacterial); 73508-07-3 (molybdenum cofactor); 9014-25-9 (RNA, Transfer); EC 2.7.7.- (MOCS3 protein, human); EC 2.7.7.- (Nucleotidyltransferases); EC 2.8.1.- (Sulfurtransferases); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (NFS1 protein, human); EC 4.4.1.- (cysteine desulfurase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00627


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[PMID]:28682051
[Au] Autor:Cornell TA; Srivastava Y; Jauch R; Fan R; Orner BP
[Ad] Endereço:Department of Chemistry, King's College London , London, U.K.
[Ti] Título:The Crystal Structure of a Maxi/Mini-Ferritin Chimera Reveals Guiding Principles for the Assembly of Protein Cages.
[So] Source:Biochemistry;56(30):3894-3899, 2017 Aug 01.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cage proteins assemble into nanoscale structures with large central cavities. They play roles, including those as virus capsids and chaperones, and have been applied to drug delivery and nanomaterials. Furthermore, protein cages have been used as model systems to understand and design protein quaternary structure. Ferritins are ubiquitous protein cages that manage iron homeostasis and oxidative damage. Two ferritin subfamilies have strongly similar tertiary structure yet distinct quaternary structure: maxi-ferritins normally assemble into 24-meric, octahedral cages with C-terminal E-helices centered around 4-fold symmetry axes, and mini-ferritins are 12-meric, tetrahedral cages with 3-fold axes defined by C-termini lacking E-domains. To understand the role E-domains play in ferritin quaternary structure, we previously designed a chimera of a maxi-ferritin E-domain fused to the C-terminus of a mini-ferritin. The chimera is a 12-mer cage midway in size between those of the maxi- and mini-ferritin. The research described herein sets out to understand (a) whether the increase in size over a typical mini-ferritin is due to a frozen state where the E-domain is flipped out of the cage and (b) whether the symmetrical preference of the E-domain in the maxi-ferritin (4-fold axis) overrules the C-terminal preference in the mini-ferritin (3-fold axis). With a 1.99 Å resolution crystal structure, we determined that the chimera assembles into a tetrahedral cage that can be nearly superimposed with the parent mini-ferritin, and that the E-domains are flipped external to the cage at the 3-fold symmetry axes.
[Mh] Termos MeSH primário: Proteínas da Membrana Bacteriana Externa/química
Proteínas de Escherichia coli/química
Metaloproteínas/química
Modelos Moleculares
[Mh] Termos MeSH secundário: Proteínas da Membrana Bacteriana Externa/genética
Proteínas da Membrana Bacteriana Externa/metabolismo
Cristalografia por Raios X
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Metaloproteínas/genética
Metaloproteínas/metabolismo
Peso Molecular
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Conformação Proteica
Conformação Proteica em alfa-Hélice
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Estrutura Quaternária de Proteína
Estrutura Terciária de Proteína
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Homologia Estrutural de Proteína
Propriedades de Superfície
Ultracentrifugação
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Escherichia coli Proteins); 0 (Metalloproteins); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 0 (bfr protein, E coli); 0 (dps protein, E coli)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170707
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00312


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[PMID]:28650996
[Au] Autor:Duncan C; Jamieson FB; Troudt J; Izzo L; Bielefeldt-Ohmann H; Izzo A; Mehaffy C
[Ad] Endereço:Public Health Ontario, Toronto, ON, Canada.
[Ti] Título:Whole transcriptomic and proteomic analyses of an isogenic M. tuberculosis clinical strain with a naturally occurring 15 Kb genomic deletion.
[So] Source:PLoS One;12(6):e0179996, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tuberculosis remains one of the most difficult to control infectious diseases in the world. Many different factors contribute to the complexity of this disease. These include the ability of the host to control the infection which may directly relate to nutritional status, presence of co-morbidities and genetic predisposition. Pathogen factors, in particular the ability of different Mycobacterium tuberculosis strains to respond to the harsh environment of the host granuloma, which includes low oxygen and nutrient availability and the presence of damaging radical oxygen and nitrogen species, also play an important role in the success of different strains to cause disease. In this study we evaluated the impact of a naturally occurring 12 gene 15 Kb genomic deletion on the physiology and virulence of M. tuberculosis. The strains denominated ON-A WT (wild type) and ON-A NM (natural mutant) were isolated from a previously reported TB outbreak in an inner city under-housed population in Toronto, Canada. Here we subjected these isogenic strains to transcriptomic (via RNA-seq) and proteomic analyses and identified several gene clusters with differential expression in the natural mutant, including the DosR regulon and the molybdenum cofactor biosynthesis genes, both of which were found in lower abundance in the natural mutant. We also demonstrated lesser virulence of the natural mutant in the guinea pig animal model. Overall, our findings suggest that the ON-A natural mutant is less fit to cause disease, but nevertheless has the potential to cause extended transmission in at-risk populations.
[Mh] Termos MeSH primário: Deleção de Genes
Genoma Bacteriano
Mycobacterium tuberculosis/genética
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/biossíntese
Proteínas de Bactérias/genética
Coenzimas/biossíntese
Coenzimas/genética
Modelos Animais de Doenças
Perfilação da Expressão Gênica
Cobaias
Seres Humanos
Metabolismo dos Lipídeos/genética
Metaloproteínas/biossíntese
Metaloproteínas/genética
Família Multigênica
Mycobacterium tuberculosis/metabolismo
Mycobacterium tuberculosis/patogenicidade
Proteínas Quinases/genética
Proteômica
Pteridinas
Regulon
Tuberculose Pulmonar/microbiologia
Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Metalloproteins); 0 (Pteridines); 73508-07-3 (molybdenum cofactor); EC 2.7.- (Protein Kinases); EC 2.7.3.- (DosR protein, Mycobacterium tuberculosis)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179996


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[PMID]:28543693
[Au] Autor:Reddy BY; Miller DM; Tsao H
[Ad] Endereço:Department of Dermatology, Wellman Center for Photomedicine, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts.
[Ti] Título:Somatic driver mutations in melanoma.
[So] Source:Cancer;123(S11):2104-2117, 2017 Jun 01.
[Is] ISSN:1097-0142
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Melanoma has one of the highest somatic mutational burdens among solid malignancies. Although the rapid progress in genomic research has contributed immensely to our understanding of the pathogenesis of melanoma, the clinical significance of the vast array of genomic alterations discovered by next-generation sequencing is far from being fully characterized. Most mutations prevalent in melanoma are simply neutral "passengers," which accompany functionally significant "drivers" under transforming conditions. The delineation of driver mutations from passenger mutations is critical to the development of targeted therapies. Novel advances in genomic data analysis have aided in distinguishing true driver mutations involved in tumor progression. Here, the authors review the current literature on important somatic driver mutations in melanoma, along with the implications for treatment. Cancer 2017;123:2104-17. © 2017 American Cancer Society.
[Mh] Termos MeSH primário: Melanoma/genética
Mutação
Neoplasias Cutâneas/genética
Neoplasias Uveais/genética
[Mh] Termos MeSH secundário: Ciclina D1/genética
GTP Fosfo-Hidrolases/genética
Subunidades alfa de Proteínas de Ligação ao GTP/genética
Subunidades alfa Gq-G11 de Proteínas de Ligação ao GTP/genética
Fatores de Troca do Nucleotídeo Guanina/genética
Sequenciamento de Nucleotídeos em Larga Escala
Seres Humanos
Proteínas de Membrana/genética
Metaloproteínas/genética
Fator de Transcrição Associado à Microftalmia/genética
Neurofibromina 1/genética
Proteínas Nucleares/genética
PTEN Fosfo-Hidrolase/genética
Proteínas Proto-Oncogênicas B-raf/genética
Proteínas Proto-Oncogênicas c-kit/genética
Proteínas de Ligação a RNA/genética
Proteínas Ribossômicas/genética
Análise de Sequência de DNA
Telomerase/genética
Proteína Supressora de Tumor p53/genética
Proteínas rac1 de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (GNA11 protein, human); 0 (GNAQ protein, human); 0 (GTP-Binding Protein alpha Subunits); 0 (Guanine Nucleotide Exchange Factors); 0 (Membrane Proteins); 0 (Metalloproteins); 0 (Microphthalmia-Associated Transcription Factor); 0 (Neurofibromin 1); 0 (Nuclear Proteins); 0 (PREX2 protein, human); 0 (RAC1 protein, human); 0 (RNA-Binding Proteins); 0 (RPS27 protein, human); 0 (Ribosomal Proteins); 0 (Tumor Suppressor Protein p53); 136601-57-5 (Cyclin D1); EC 2.7.10.1 (Proto-Oncogene Proteins c-kit); EC 2.7.11.1 (Proto-Oncogene Proteins B-raf); EC 2.7.7.49 (TERT protein, human); EC 2.7.7.49 (Telomerase); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (NRAS protein, human); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gq-G11); EC 3.6.5.2 (rac1 GTP-Binding Protein)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1002/cncr.30593


  8 / 5866 MEDLINE  
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[PMID]:28511095
[Au] Autor:Cho S; Jung SE; Hong SR; Lee EH; Lee JH; Lee SD; Lee HY
[Ad] Endereço:Institute of Forensic Science, Seoul National University College of Medicine, Seoul, Korea.
[Ti] Título:Independent validation of DNA-based approaches for age prediction in blood.
[So] Source:Forensic Sci Int Genet;29:250-256, 2017 Jul.
[Is] ISSN:1878-0326
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Numerous molecular biomarkers have been proposed as predictors of chronological age. Among them, T-cell specific DNA rearrangement and DNA methylation markers have been introduced as forensic age predictors in blood because of their high prediction accuracy. These markers appear highly promising, but for better application to forensic casework sample analysis the proposed markers and genotyping methods must be tested further. In the current study, signal-joint T-cell receptor excision circles (sjTRECs) and DNA methylation markers located in the ELOVL2, C1orf132, TRIM59, KLF14, and FHL2 genes were reanalyzed in 100 Korean blood samples to test their associations with chronological age, using the same analysis platform used in previous reports. Our study replicated the age association test for sjTREC and DNA methylation markers in the 5 genes in an independent validation set of 100 Koreans, and proved that the age predictive performance of the previous models is relatively consistent across different population groups. However, the extent of age association at certain CpG loci was not identical in the Korean and Polish populations; therefore, several age predictive models were retrained with the data obtained here. All of the 3 models retrained with DNA methylation and/or sjTREC data have a CpG site each from the ELOVL2 and FHL2 genes in common, and produced better prediction accuracy than previously reported models. This is attributable to the fact that the retrained model better fits the existing data and that the calculated prediction accuracy could be higher when the training data and the test data are the same. However, it is notable that the combination of different types of markers, i.e., sjTREC and DNA methylation, improved prediction accuracy in the eldest group. Our study demonstrates the usefulness of the proposed markers and the genotyping method in an independent dataset, and suggests the possibility of combining different types of DNA markers to improve prediction accuracy.
[Mh] Termos MeSH primário: Envelhecimento/genética
Metilação de DNA
Marcadores Genéticos
Receptores de Antígenos de Linfócitos T/sangue
[Mh] Termos MeSH secundário: Acetiltransferases/genética
Grupo com Ancestrais do Continente Asiático/genética
Ilhas de CpG/genética
Técnicas de Genotipagem
Seres Humanos
Proteínas com Homeodomínio LIM/genética
Proteínas de Membrana/genética
Metaloproteínas/genética
Proteínas Musculares/genética
Receptores de Antígenos de Linfócitos T/genética
República da Coreia
Fatores de Transcrição Sp/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (FHL2 protein, human); 0 (Genetic Markers); 0 (KLF14 protein, human); 0 (LIM-Homeodomain Proteins); 0 (Membrane Proteins); 0 (Metalloproteins); 0 (Muscle Proteins); 0 (Receptors, Antigen, T-Cell); 0 (Sp Transcription Factors); 0 (TRIM59 protein, human); 0 (Transcription Factors); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (fatty acid elongases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170707
[Lr] Data última revisão:
170707
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE


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[PMID]:28485213
[Au] Autor:Kitajima S; Imamura T; Iibushi J; Ikenaga M; Tachibana Y; Andoh N; Oyabu H; Hirooka K; Shiina T; Ishizaki Y
[Ad] Endereço:a Department of Applied Biology , Kyoto Institute of Technology , Kyoto , Japan.
[Ti] Título:Ferritin 2 domain-containing protein found in lacquer tree (Toxicodendron vernicifluum) sap has negative effects on laccase and peroxidase reactions.
[So] Source:Biosci Biotechnol Biochem;81(6):1165-1175, 2017 Jun.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lacquer tree sap, a raw material of traditional paints in East Asia, is hardened through laccase-catalyzed oxidation and the following polymerization of phenolic compound urushiol. In the sap's water-insoluble fraction, we found two plantacyanins and a ferritin 2 domain-containing protein (TvFe2D, a homolog of Arabidopsis AT1G47980 and AT3G62730). The recombinant TvFe2D protein suppressed the accumulation of laccase-catalyzed oxidation products of a model substrate syringaldazine without decreasing oxygen consumption, the second substrate of laccase. The suppression was also observed when another substrate guaiacol or another oxidizing enzyme peroxidase was used. The functional domain of the suppression was the C-terminal half, downstream of the ferritin 2 domain. The results suggest that this protein may be involved in regulating the sap polymerization/hardening. We also discuss the possibility that homologous proteins of TvFe2D in other plants might be involved in the laccase- or peroxidase-mediated polymerization of phenolic compounds, such as lignin and flavonoids.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica de Plantas
Lacase/metabolismo
Laca/análise
Metaloproteínas/metabolismo
Peroxidases/metabolismo
Proteínas de Plantas/metabolismo
Toxicodendron/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Biocatálise
Catecóis/metabolismo
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Ferritinas/química
Guaiacol/metabolismo
Hidrazonas/metabolismo
Cinética
Lacase/genética
Lignina/metabolismo
Metaloproteínas/genética
Oxirredução
Consumo de Oxigênio
Peroxidases/genética
Proteínas de Plantas/genética
Polimerização
Domínios Proteicos
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Toxicodendron/química
Árvores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Catechols); 0 (Hydrazones); 0 (Metalloproteins); 0 (Plant Proteins); 0 (Recombinant Proteins); 14414-32-5 (syringaldazine); 53237-59-5 (urushiol); 6JKA7MAH9C (Guaiacol); 9005-53-2 (Lignin); 9007-73-2 (Ferritins); EC 1.10.3.2 (Laccase); EC 1.11.1.- (Peroxidases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170703
[Lr] Data última revisão:
170703
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170510
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1289814


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[PMID]:28441529
[Au] Autor:Maciejowski J; Drechsler H; Grundner-Culemann K; Ballister ER; Rodriguez-Rodriguez JA; Rodriguez-Bravo V; Jones MJK; Foley E; Lampson MA; Daub H; McAinsh AD; Jallepalli PV
[Ad] Endereço:Molecular Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA; Louis V. Gerstner, Jr. Graduate School of Biomedical Sciences, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
[Ti] Título:Mps1 Regulates Kinetochore-Microtubule Attachment Stability via the Ska Complex to Ensure Error-Free Chromosome Segregation.
[So] Source:Dev Cell;41(2):143-156.e6, 2017 Apr 24.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The spindle assembly checkpoint kinase Mps1 not only inhibits anaphase but also corrects erroneous attachments that could lead to missegregation and aneuploidy. However, Mps1's error correction-relevant substrates are unknown. Using a chemically tuned kinetochore-targeting assay, we show that Mps1 destabilizes microtubule attachments (K fibers) epistatically to Aurora B, the other major error-correcting kinase. Through quantitative proteomics, we identify multiple sites of Mps1-regulated phosphorylation at the outer kinetochore. Substrate modification was microtubule sensitive and opposed by PP2A-B56 phosphatases that stabilize chromosome-spindle attachment. Consistently, Mps1 inhibition rescued K-fiber stability after depleting PP2A-B56. We also identify the Ska complex as a key effector of Mps1 at the kinetochore-microtubule interface, as mutations that mimic constitutive phosphorylation destabilized K fibers in vivo and reduced the efficiency of the Ska complex's conversion from lattice diffusion to end-coupled microtubule binding in vitro. Our results reveal how Mps1 dynamically modifies kinetochores to correct improper attachments and ensure faithful chromosome segregation.
[Mh] Termos MeSH primário: Segregação de Cromossomos/fisiologia
Cinetocoros/metabolismo
Metaloproteínas/metabolismo
Microtúbulos/metabolismo
Mitose/fisiologia
Proteínas Nucleares/metabolismo
Proteínas de Ligação a RNA/metabolismo
Proteínas Ribossômicas/metabolismo
[Mh] Termos MeSH secundário: Anáfase/fisiologia
Aurora Quinase B/metabolismo
Proteínas de Ciclo Celular/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Seres Humanos
Pontos de Checagem da Fase M do Ciclo Celular/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Chromosomal Proteins, Non-Histone); 0 (Metalloproteins); 0 (Nuclear Proteins); 0 (RNA-Binding Proteins); 0 (RPS27 protein, human); 0 (Ribosomal Proteins); 0 (SKA1 protein, human); EC 2.7.11.1 (Aurora Kinase B)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170426
[St] Status:MEDLINE



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