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[PMID]:28581380
[Au] Autor:Oksanen HM; Ictv Report Consortium
[Ad] Endereço:Department of Biosciences and Institute of Biotechnology, University of Helsinki, FIN-00014 Helsinki, Finland.
[Ti] Título:ICTV Virus Taxonomy Profile: Corticoviridae.
[So] Source:J Gen Virol;98(5):888-889, 2017 May.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Corticoviridae is a family of icosahedral, internal-membrane-containing viruses with double-stranded circular DNA genomes of approximately 10 kb. Only one species, Pseudoalteromonas virus PM2, has been recognized. Pseudoalteromonas virus PM2 infects Gram-negative bacteria and was isolated from seawater in 1968. Pseudoalteromonas virus PM2 is the first bacterial virus in which the presence of lipids in the virion has been demonstrated. Viral lipids are acquired selectively during virion assembly from the host cytoplasmic membrane. The outer protein capsid is an icosahedron with a pseudo T=21 symmetry. This is a summary of the International Committee on Taxonomy of Viruses (ICTV) Report on the taxonomy of the Corticoviridae, which is available at www.ictv.global/report/corticoviridae.
[Mh] Termos MeSH primário: Corticoviridae/química
Corticoviridae/classificação
[Mh] Termos MeSH secundário: Corticoviridae/genética
Corticoviridae/isolamento & purificação
Genoma Viral
Vírion/química
Vírion/classificação
Vírion/genética
Vírion/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000795


  2 / 33 MEDLINE  
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[PMID]:25775825
[Au] Autor:Andreev VM; Kuznetsova NV; Shevelev AB; Kudykina IuK; Guseva MA; Epremian AS; Lisitsyna ES; Kuz'min VA
[Ti] Título:[Photosensitizing properties of 3,3'-diethylthiacarbocyanine in biological media].
[So] Source:Radiats Biol Radioecol;54(4):367-76, 2014 Jul-Aug.
[Is] ISSN:0869-8031
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:The objective of the study is elucidation of perspectives of 3,3'-diathylcarbocyaine application as a photosensitizer for curing viral infections by photodynamic therapy. Lipid-containing bacteriophage PM-2 of Pseudoalteromonas espejiana was used as a model. The testing was carried out at a special installation modeling photodynamic exposure conditions towards a non-fractionated phage lysate. 3,3'-DECC demonstrated a rapid photo-bleaching when added tothe phage lysate but not to water. The initial rate of PM-2 phage photoinactivation was proportional to the square concentration of the dye in the range of 0.5-9 µmol/L. This confirms a hypothesis that the dimer is the principal photochemically active form of the dye. An improved ability to form dimers was found in the dye in the phage lysate (10-folds better than in the water). The dye formed a stable adduct with the bacteriophage material. This adduct had an extinction maximum at λ(max) = 594 nm and demonstrated the properties of a polymer (sedimentation under a low-speed centrifugation).
[Mh] Termos MeSH primário: Benzotiazóis/farmacologia
Carbocianinas/farmacologia
Corticoviridae/efeitos dos fármacos
Modelos Biológicos
Fotoquimioterapia/métodos
Fármacos Fotossensibilizantes/farmacologia
[Mh] Termos MeSH secundário: Benzotiazóis/química
Benzotiazóis/uso terapêutico
Carbocianinas/química
Carbocianinas/uso terapêutico
Corticoviridae/efeitos da radiação
Dimerização
Fármacos Fotossensibilizantes/química
Fármacos Fotossensibilizantes/uso terapêutico
Pseudoalteromonas/virologia
Viroses/tratamento farmacológico
Viroses/radioterapia
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzothiazoles); 0 (Carbocyanines); 0 (Photosensitizing Agents); 905-97-5 (3,3'-diethylthiacarbocyanine iodide)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:161020
[Lr] Data última revisão:
161020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150318
[St] Status:MEDLINE


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[PMID]:24189238
[Au] Autor:Stuart DI; Abrescia NG
[Ad] Endereço:Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7BN, England.
[Ti] Título:From lows to highs: using low-resolution models to phase X-ray data.
[So] Source:Acta Crystallogr D Biol Crystallogr;69(Pt 11):2257-65, 2013 Nov.
[Is] ISSN:1399-0047
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The study of virus structures has contributed to methodological advances in structural biology that are generally applicable (molecular replacement and noncrystallographic symmetry are just two of the best known examples). Moreover, structural virology has been instrumental in forging the more general concept of exploiting phase information derived from multiple structural techniques. This hybridization of structural methods, primarily electron microscopy (EM) and X-ray crystallography, but also small-angle X-ray scattering (SAXS) and nuclear magnetic resonance (NMR) spectroscopy, is central to integrative structural biology. Here, the interplay of X-ray crystallography and EM is illustrated through the example of the structural determination of the marine lipid-containing bacteriophage PM2. Molecular replacement starting from an ~13 Å cryo-EM reconstruction, followed by cycling density averaging, phase extension and solvent flattening, gave the X-ray structure of the intact virus at 7 Å resolution This in turn served as a bridge to phase, to 2.5 Å resolution, data from twinned crystals of the major coat protein (P2), ultimately yielding a quasi-atomic model of the particle, which provided significant insights into virus evolution and viral membrane biogenesis.
[Mh] Termos MeSH primário: Substituição de Aminoácidos
Proteínas do Capsídeo/química
Corticoviridae/química
Modelos Moleculares
Espalhamento a Baixo Ângulo
[Mh] Termos MeSH secundário: Bromus/química
Bromus/ultraestrutura
Bromus/virologia
Proteínas do Capsídeo/ultraestrutura
Corticoviridae/ultraestrutura
Microscopia Crioeletrônica/métodos
Microscopia Crioeletrônica/tendências
Cristalização
Cristalografia por Raios X
Espectroscopia de Ressonância Magnética
Vírus do Mosaico do Tabaco/química
Vírus do Mosaico do Tabaco/ultraestrutura
Vírus Satélite da Necrose do Tabaco/química
Vírus Satélite da Necrose do Tabaco/ultraestrutura
Tombusvirus/química
Tombusvirus/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Capsid Proteins)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131106
[St] Status:MEDLINE
[do] DOI:10.1107/S0907444913022336


  4 / 33 MEDLINE  
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[PMID]:23842892
[Au] Autor:Vignoni M; Rasse-Suriani FA; Butzbach K; Erra-Balsells R; Epe B; Cabrerizo FM
[Ad] Endereço:Instituto de Investigaciones Biotecnológicas - Instituto Tecnológico de Chascomús (IIB-INTECH), Universidad Nacional de San Martín (UNSAM) - Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Intendente Marino Km 8.2, CC 164 (B7130IWA), Chascomús, Argentina.
[Ti] Título:Mechanisms of DNA damage by photoexcited 9-methyl-ß-carbolines.
[So] Source:Org Biomol Chem;11(32):5300-9, 2013 Aug 28.
[Is] ISSN:1477-0539
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:It has been well documented that ß-carboline alkaloids, particularly the 9-methyl derivatives, are efficient photosensitizers. However, structure-activity relationships are missing and the photochemical mechanisms involved in the DNA photodamage still remain unknown. In the present work, we examined the capability of three 9-methyl-ß-carbolines (9-methyl-norharmane, 9-methyl-harmane and 9-methyl-harmine) to induce DNA damage upon UVA excitation at physiological pH. The type and extent of the damage was analyzed together with the photophysical and binding properties of the ß-carboline derivatives investigated. The results indicate that even at neutral pH most of the DNA damage is generated from the protonated form of the excited ß-carbolines in a type-I reaction. Oxidized purine residues are produced in high excess over oxidized pyrimidines, single-strand breaks and sites of base loss. In addition, the excited neutral form of the ß-carbolines is responsible for significant generation of cyclobutane pyrimidine dimers (CPDs) by triplet-triplet-energy transfer. In the case of 9-methyl-norharmane, the yield of CPDs is increased in D2O, probably due to less rapid protonation in the deuterated solvent.
[Mh] Termos MeSH primário: Carbolinas/farmacologia
Corticoviridae/genética
Dano ao DNA/efeitos dos fármacos
DNA Viral/genética
DNA/genética
Fármacos Fotossensibilizantes/farmacologia
[Mh] Termos MeSH secundário: Animais
Carbolinas/química
Bovinos
Modelos Moleculares
Fármacos Fotossensibilizantes/química
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (9-methyl-beta-carboline); 0 (Carbolines); 0 (DNA, Viral); 0 (Photosensitizing Agents); 9007-49-2 (DNA); 91080-16-9 (calf thymus DNA)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:130724
[Lr] Data última revisão:
130724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130712
[St] Status:MEDLINE
[do] DOI:10.1039/c3ob40344k


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[PMID]:21742267
[Au] Autor:Bahar MW; Graham SC; Stuart DI; Grimes JM
[Ad] Endereço:The Division of Structural Biology and the Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, UK.
[Ti] Título:Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13.
[So] Source:Structure;19(7):1011-20, 2011 Jul 13.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The morphogenesis of poxviruses such as vaccinia virus (VACV) sees the virion shape mature from spherical to brick-shaped. Trimeric capsomers of the VACV D13 protein form a transitory, stabilizing lattice on the surface of the initial spherical immature virus particle. The crystal structure of D13 reveals that this major scaffolding protein comprises a double ß barrel "jelly-roll" subunit arranged as pseudo-hexagonal trimers. These structural features are characteristic of the major capsid proteins of a lineage of large icosahedral double-stranded DNA viruses including human adenovirus and the bacteriophages PRD1 and PM2. Structure-based phylogenetic analysis confirms that VACV belongs to this lineage, suggesting that (analogously to higher organism embryogenesis) early poxvirus morphogenesis reflects their evolution from a lineage of viruses sharing a common icosahedral ancestor.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/química
Capsídeo/química
Proteínas Recombinantes de Fusão/química
Vírus Vaccinia/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bacteriófago PRD1/química
Evolução Biológica
Capsídeo/metabolismo
Proteínas do Capsídeo/genética
Proteínas do Capsídeo/metabolismo
Clonagem Molecular
Corticoviridae/química
Cristalização
Cristalografia por Raios X
Seres Humanos
Modelos Moleculares
Dados de Sequência Molecular
Filogenia
Plasmídeos
Conformação Proteica
Estrutura Secundária de Proteína
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Transfecção
Vaccinia/virologia
Vírus Vaccinia/genética
Vírus Vaccinia/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Recombinant Fusion Proteins)
[Em] Mês de entrada:1111
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110712
[St] Status:MEDLINE
[do] DOI:10.1016/j.str.2011.03.023


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[PMID]:20646729
[Au] Autor:Cvirkaite-Krupovic V; Krupovic M; Daugelavicius R; Bamford DH
[Ad] Endereço:Department of Biosciences and Institute of Biotechnology, University of Helsinki, Finland.
[Ti] Título:Calcium ion-dependent entry of the membrane-containing bacteriophage PM2 into its Pseudoalteromonas host.
[So] Source:Virology;405(1):120-8, 2010 Sep 15.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Marine bacteriophage PM2 infects gram-negative Pseudoalteromonas species and is currently the only assigned member of the Corticoviridae family. The icosahedral protein shell covers an internal protein-rich phage membrane that encloses the highly supercoiled dsDNA genome. In this study we investigated PM2 entry into the host. Our results indicate that PM2 adsorption to the host is dependent on the intracellular ATP concentration, while genome penetration through the cytoplasmic membrane depends on the presence of millimolar concentrations of calcium ions in the medium. In the absence of Ca(2+) the infection is arrested at the entry stage but can be rescued by the addition of Ca(2+). Interestingly, PM2 entry induces abrupt cell lysis if the host outer membrane is not stabilized by divalent cations. Experimental data described in this study in combination with results obtained previously allowed us to propose a sequential model describing the entry of bacteriophage PM2 into the host cells.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Corticoviridae/fisiologia
Pseudoalteromonas/virologia
Internalização do Vírus
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Membrana Celular
Receptores de Superfície Celular
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Receptors, Cell Surface); 8L70Q75FXE (Adenosine Triphosphate); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1008
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100722
[St] Status:MEDLINE
[do] DOI:10.1016/j.virol.2010.05.021


  7 / 33 MEDLINE  
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[PMID]:18775333
[Au] Autor:Abrescia NG; Grimes JM; Kivelä HM; Assenberg R; Sutton GC; Butcher SJ; Bamford JK; Bamford DH; Stuart DI
[Ad] Endereço:Division of Structural Biology and the Oxford Protein Production Facility, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7BN, UK.
[Ti] Título:Insights into virus evolution and membrane biogenesis from the structure of the marine lipid-containing bacteriophage PM2.
[So] Source:Mol Cell;31(5):749-61, 2008 Sep 05.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent, primarily structural observations indicate that related viruses, harboring no sequence similarity, infect hosts of different domains of life. One such clade of viruses, defined by common capsid architecture and coat protein fold, is the so-called PRD1-adenovirus lineage. Here we report the structure of the marine lipid-containing bacteriophage PM2 determined by crystallographic analyses of the entire approximately 45 MDa virion and of the outer coat proteins P1 and P2, revealing PM2 to be a primeval member of the PRD1-adenovirus lineage with an icosahedral shell and canonical double beta barrel major coat protein. The view of the lipid bilayer, richly decorated with membrane proteins, constitutes a rare visualization of an in vivo membrane. The viral membrane proteins P3 and P6 are organized into a lattice, suggesting a possible assembly pathway to produce the mature virus.
[Mh] Termos MeSH primário: Evolução Biológica
Proteínas do Capsídeo/química
Corticoviridae/ultraestrutura
Lipídeos/química
Vírus/genética
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Proteínas do Capsídeo/classificação
Proteínas do Capsídeo/genética
Proteínas do Capsídeo/metabolismo
Corticoviridae/química
Cristalografia por Raios X
Modelos Moleculares
Dados de Sequência Molecular
Conformação Proteica
Vírion/química
Vírion/ultraestrutura
Vírus/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Lipids); SY7Q814VUP (Calcium)
[Em] Mês de entrada:0809
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080909
[St] Status:MEDLINE
[do] DOI:10.1016/j.molcel.2008.06.026


  8 / 33 MEDLINE  
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[PMID]:18083813
[Au] Autor:Kivelä HM; Madonna S; Krupovìc M; Tutino ML; Bamford JK
[Ad] Endereço:Department of Biological and Environmental Science and Nanoscience Center, University of Jyväskylä, Jyväskylä, Finland.
[Ti] Título:Genetics for Pseudoalteromonas provides tools to manipulate marine bacterial virus PM2.
[So] Source:J Bacteriol;190(4):1298-307, 2008 Feb.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The genetic manipulation of marine double-stranded DNA (dsDNA) bacteriophage PM2 (Corticoviridae) has been limited so far. The isolation of an autonomously replicating DNA element of Pseudoalteromonas haloplanktis TAC125 and construction of a shuttle vector replicating in both Escherichia coli and Pseudoalteromonas enabled us to design a set of conjugative shuttle plasmids encoding tRNA suppressors for amber mutations. Using a host strain carrying a suppressor plasmid allows the introduction and analysis of nonsense mutations in PM2. Here, we describe the isolation and characterization of a suppressor-sensitive PM2 sus2 mutant deficient in the structural protein P10. To infect and replicate, PM2 delivers its 10-kbp genome across the cell envelopes of two gram-negative Pseudoalteromonas species. The events leading to the internalization of the circular supercoiled dsDNA are puzzling. In a poorly understood process that follows receptor recognition, the virion capsid disassembles and the internal membrane fuses with the host outer membrane. While beginning to unravel the mechanism of this process, we found that protein P10 plays an essential role in the host cell penetration.
[Mh] Termos MeSH primário: Corticoviridae/genética
Pseudoalteromonas/virologia
[Mh] Termos MeSH secundário: Proteínas do Capsídeo/genética
Corticoviridae/crescimento & desenvolvimento
Corticoviridae/isolamento & purificação
DNA Circular/genética
Eletroforese em Gel de Poliacrilamida
Escherichia coli/genética
Escherichia coli/virologia
Vetores Genéticos/genética
Genoma Viral/genética
Modelos Genéticos
Mutagênese Sítio-Dirigida
Mutação
Fenótipo
Plasmídeos/genética
Pseudoalteromonas/genética
RNA de Transferência/genética
Água do Mar/virologia
Proteínas Virais/genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (DNA, Circular); 0 (Viral Proteins); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:0807
[Cu] Atualização por classe:140904
[Lr] Data última revisão:
140904
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:071218
[St] Status:MEDLINE


  9 / 33 MEDLINE  
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[PMID]:18082422
[Au] Autor:Kivelä HM; Abrescia NG; Bamford JK; Grimes JM; Stuart DI; Bamford DH
[Ad] Endereço:Department of Biological and Environmental Science and Nanoscience Centre, University of Jyväskylä, P.O. Box 35 (Survontie 9), 40014 Jyväskylä, Finland.
[Ti] Título:Selenomethionine labeling of large biological macromolecular complexes: probing the structure of marine bacterial virus PM2.
[So] Source:J Struct Biol;161(2):204-10, 2008 Feb.
[Is] ISSN:1095-8657
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There is a need for improved tools for labeling protein species within large macromolecular assemblies. Here we describe a method for the efficient selenomethionine labeling of the membrane-containing bacterial virus PM2 for structural studies. By examining potential host cells a strain was found which was auxotrophic for methionine, and by performing a multiparameter search of conditions it was possible to derive a robust protocol which simultaneously minimized the toxic effects of the selenomethionine, so that a reasonable virus yield was maintained, whilst still achieving essentially complete labeling. This has allowed us to fingerprint the protein constituents of the virus in a relatively low resolution electron density map. Such a technique can be adapted to other macromolecule complexes studied by X-ray crystallography.
[Mh] Termos MeSH primário: Corticoviridae/química
Corticoviridae/ultraestrutura
Selenometionina/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
964MRK2PEL (Selenomethionine)
[Em] Mês de entrada:0803
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:071218
[St] Status:MEDLINE


  10 / 33 MEDLINE  
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[PMID]:17675188
[Au] Autor:Trapp C; McCullough AK; Epe B
[Ad] Endereço:Institute of Pharmacy, University of Mainz, D-55099 Mainz, Germany.
[Ti] Título:The basal levels of 8-oxoG and other oxidative modifications in intact mitochondrial DNA are low even in repair-deficient (Ogg1(-/-)/Csb(-/-)) mice.
[So] Source:Mutat Res;625(1-2):155-63, 2007 Dec 01.
[Is] ISSN:0027-5107
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mitochondrial DNA (mtDNA) is assumed to be highly prone to damage by reactive oxygen species (ROS) because of its location in close proximity to the mitochondrial electron transport chain. Accordingly, mitochondrial oxidative DNA damage has been hypothesized to be responsible for various neurological diseases, ageing and cancer. Since 7,8-dihydro-8-oxoguanine (8-oxoG), one of the most frequent oxidative base modifications, is removed from the mitochondrial genome by the glycosylase OGG1, the basal levels of this lesion are expected to be highly elevated in Ogg1(-/-) mice. To investigate this hypothesis, we have used a mtDNA relaxation assay in combination with various repair enzymes (Fpg, MutY, endonuclease III, endonuclease IV) to determine the average steady-state number of oxidative DNA modifications within intact (supercoiled) mtDNA from the livers of wild-type mice and those deficient in OGG1 and/or the Cockayne syndrome B (CSB) protein for mice aged up to 23 months. The levels of all types of oxidative modifications were found to be less than 12 per million base pairs, and the difference between wild-type and repair-deficient (Ogg1(-/-)/Csb(-/-)) mice was not significant. Thus, the increase of 8-oxoG caused by the repair deficiency in intact mtDNA is not much higher than in the nuclear DNA, i.e., not more than a few modifications per million base pairs. Based on these data, it is hypothesized that the load of oxidative base modifications in mtDNA is efficiently reduced during replication even in the absence of excision repair.
[Mh] Termos MeSH primário: DNA Glicosilases/deficiência
Enzimas Reparadoras do DNA/deficiência
Reparo do DNA/fisiologia
DNA Mitocondrial/metabolismo
Guanosina/análogos & derivados
[Mh] Termos MeSH secundário: Animais
Corticoviridae/metabolismo
Dano ao DNA
DNA Glicosilases/genética
Reparo do DNA/genética
Enzimas Reparadoras do DNA/genética
Enzimas Reparadoras do DNA/metabolismo
DNA Mitocondrial/química
DNA Viral/química
DNA Viral/metabolismo
Feminino
Guanosina/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Extratos Vegetais/metabolismo
Proteínas de Ligação a Poli-ADP-Ribose
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (DNA, Viral); 0 (LI 1370); 0 (Plant Extracts); 0 (Poly-ADP-Ribose Binding Proteins); 12133JR80S (Guanosine); 3868-31-3 (8-hydroxyguanosine); EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (Ogg1 protein, mouse); EC 3.6.4.12 (Ercc6 protein, mouse); EC 6.5.1.- (DNA Repair Enzymes)
[Em] Mês de entrada:0712
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:070807
[St] Status:MEDLINE



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