Base de dados : MEDLINE
Pesquisa : B02.200.850.800 [Categoria DeCS]
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[PMID]:28342228
[Au] Autor:Mallik S; Kundu S
[Ad] Endereço:Department of Biophysics, Molecular Biology and Bioinformatics, University of Calcutta, Kolkata, West Bengal, India.
[Ti] Título:Coevolutionary constraints in the sequence-space of macromolecular complexes reflect their self-assembly pathways.
[So] Source:Proteins;85(7):1183-1189, 2017 Jul.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Is the order in which biomolecular subunits self-assemble into functional macromolecular complexes imprinted in their sequence-space? Here, we demonstrate that the temporal order of macromolecular complex self-assembly can be efficiently captured using the landscape of residue-level coevolutionary constraints. This predictive power of coevolutionary constraints is irrespective of the structural, functional, and phylogenetic classification of the complex and of the stoichiometry and quaternary arrangement of the constituent monomers. Combining this result with a number of structural attributes estimated from the crystal structure data, we find indications that stronger coevolutionary constraints at interfaces formed early in the assembly hierarchy probably promotes coordinated fixation of mutations that leads to high-affinity binding with higher surface area, increased surface complementarity and elevated number of molecular contacts, compared to those that form late in the assembly. Proteins 2017; 85:1183-1189. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Evolução Molecular
Multimerização Proteica
Subunidades Proteicas/química
Proteínas/química
[Mh] Termos MeSH secundário: Bactérias/química
Conjuntos de Dados como Assunto
Modelos Moleculares
Oryza/química
Domínios Proteicos
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Termodinâmica
Thermoplasma/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); 0 (Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170326
[St] Status:MEDLINE
[do] DOI:10.1002/prot.25292


  2 / 444 MEDLINE  
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[PMID]:28302716
[Au] Autor:Ogino H; Ishino S; Kohda D; Ishino Y
[Ad] Endereço:From the Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, 6-10-1 Hakozaki, Higashiku, Fukuoka 812-8581, Japan and.
[Ti] Título:The RecJ2 protein in the thermophilic archaeon is a 3'-5' exonuclease that associates with a DNA replication complex.
[So] Source:J Biol Chem;292(19):7921-7931, 2017 May 12.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RecJ/cell division cycle 45 (Cdc45) proteins are widely conserved in the three domains of life, in bacteria, Eukarya, and Archaea. Bacterial RecJ is a 5'-3' exonuclease and functions in DNA repair pathways by using its 5'-3' exonuclease activity. Eukaryotic Cdc45 has no identified enzymatic activity but participates in the CMG complex, so named because it is composed of Cdc45, minichromosome maintenance protein complex (MCM) proteins 2-7, and GINS complex proteins (Sld5, Psf11-3). Eukaryotic Cdc45 and bacterial/archaeal RecJ share similar amino acid sequences and are considered functional counterparts. In Archaea, a RecJ homolog in was shown to associate with GINS and accelerate its nuclease activity and was, therefore, designated GAN ( INS- ssociated uclease); however, to date, no archaeal RecJ·MCM·GINS complex has been isolated. The thermophilic archaeon has two RecJ-like proteins, designated TaRecJ1 and TaRecJ2. TaRecJ1 exhibited DNA-specific 5'-3' exonuclease activity, whereas TaRecJ2 had 3'-5' exonuclease activity and preferred RNA over DNA. TaRecJ2, but not TaRecJ1, formed a stable complex with TaGINS in a 2:1 molar ratio. Furthermore, the TaRecJ2·TaGINS complex stimulated activity of TaMCM ( MCM) helicase , and the TaRecJ2·TaMCM·TaGINS complex was also observed However, TaRecJ2 did not interact with TaMCM directly and was not required for the helicase activation These findings suggest that the function of archaeal RecJ in DNA replication evolved divergently from Cdc45 despite conservation of the CMG-like complex formation between Archaea and Eukarya.
[Mh] Termos MeSH primário: Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Replicação do DNA
Endodesoxirribonucleases/genética
Exonucleases/metabolismo
Thermoplasma/enzimologia
[Mh] Termos MeSH secundário: Proteínas de Ciclo Celular/metabolismo
Clonagem Molecular
DNA Helicases/metabolismo
Reparo do DNA
DNA Arqueal/química
Proteínas de Ligação a DNA/metabolismo
Desoxirribonucleases/metabolismo
Endodesoxirribonucleases/metabolismo
Concentração de Íons de Hidrogênio
Imunoprecipitação
Oligonucleotídeos/química
Ligação Proteica
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Cell Cycle Proteins); 0 (DNA, Archaeal); 0 (DNA-Binding Proteins); 0 (Oligonucleotides); 0 (Recombinant Proteins); EC 3.1.- (Deoxyribonucleases); EC 3.1.- (Endodeoxyribonucleases); EC 3.1.- (Exonucleases); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170318
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.767921


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[PMID]:27799846
[Au] Autor:Fujii M; Hata C; Ukita M; Fukushima C; Matsuura C; Kawashima-Ohya Y; Tomobe K; Kawashima T
[Ad] Endereço:Department of Molecular Biology, Faculty of Pharmaceutical Science, Yokohama University of Pharmacy, 601 Matano-cho, Totsuka-ku, Yokohama 245-0066, Japan.
[Ti] Título:Characterization of a Thermostable 8-Oxoguanine DNA Glycosylase Specific for GO/N Mismatches from the Thermoacidophilic Archaeon .
[So] Source:Archaea;2016:8734894, 2016.
[Is] ISSN:1472-3654
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The oxidation of guanine (G) to 7,8-dihydro-8-oxoguanine (GO) forms one of the major DNA lesions generated by reactive oxygen species (ROS). The GO can be corrected by GO DNA glycosylases (Ogg), enzymes involved in base excision repair (BER). Unrepaired GO induces mismatched base pairing with adenine (A); as a result, the mismatch causes a point mutation, from G paired with cytosine (C) to thymine (T) paired with adenine (A), during DNA replication. Here, we report the characterization of a putative Ogg from the thermoacidophilic archaeon . The 204-amino acid sequence of the putative Ogg (TVG_RS00315) shares significant sequence homology with the DNA glycosylases of (MjaOgg) and (SsoOgg). The six histidine-tagged recombinant TVG_RS00315 protein gene was expressed in and purified. The Ogg protein is thermostable, with optimal activity near a pH of 7.5 and a temperature of 60°C. The enzyme displays DNA glycosylase, and apurinic/apyrimidinic (AP) lyase activities on GO/N (where N is A, T, G, or C) mismatch; yet it cannot eliminate U from U/G or T from T/G, as mismatch glycosylase (MIG) can. These results indicate that TvoOgg-encoding is a member of the Ogg2 family of .
[Mh] Termos MeSH primário: DNA Glicosilases/metabolismo
DNA/metabolismo
Guanina/análogos & derivados
Thermoplasma/enzimologia
[Mh] Termos MeSH secundário: DNA Glicosilases/química
DNA Glicosilases/genética
Estabilidade Enzimática
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Guanina/metabolismo
Concentração de Íons de Hidrogênio
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Temperatura Ambiente
Thermoplasma/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (7,8-dihydro-8-oxoguanine); 0 (Recombinant Proteins); 5Z93L87A1R (Guanine); 9007-49-2 (DNA); EC 3.2.2.- (DNA Glycosylases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161102
[St] Status:MEDLINE


  4 / 444 MEDLINE  
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[PMID]:27405311
[Au] Autor:Nagy I; Knispel RW; Kofler C; Orsini M; Boicu M; Varga S; Weyher-Stingl E; Sun N; Fernandez-Busnadiego R; Kukolya J; Nickell S; Baumeister W
[Ad] Endereço:Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried (Planegg), Germany nagy@biochem.mpg.de.
[Ti] Título:Lipoprotein-like particles in a prokaryote: quinone droplets of Thermoplasma acidophilum.
[So] Source:FEMS Microbiol Lett;363(18), 2016 Sep.
[Is] ISSN:1574-6968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cytosolic, globular droplets with an average diameter of 50 nm were observed in vitrified Thermoplasma acidophilum cells by means of cryo-electron tomography. These droplets were isolated by column chromatography and immunoprecipitation protein purification methods. Subsequent chemical and biochemical analyses identified lipid and protein components, respectively. Two major lipid components, comigrating menaquinones at the solvent front and the slower migrating Thermoplasma polar lipid U4, were detected by TLC experiments. The major protein component was identified as the 153 amino acid long Ta0547 vitellogenin-N domain protein. This domain has been found so far exclusively in large lipid transport proteins of vertebrates and non-vertebrates. Blast protein database homology searches with Ta0547 did not return any eukaryal hits; homologous sequences were found only in thermo-acidophilic archaeons. However, a profile-sequence domain search performed with the vitellogenin-N domain (PF01347) hmm-profile against the T. acidophilum proteome returned Ta0547 as hit. Electron microscopy appearance of isolated droplets resembled to lipoprotein particles. However, no (tetraether) lipid layer could be detected on the droplets surface, rather hydrophobic compounds of the electron dense lumen were surrounded by a denser discontinuous protein boundary. Based on described features, these particles qualify for a novel lipoprotein particle category, what we nominated Thermoplasma Quinone Droplet.
[Mh] Termos MeSH primário: Benzoquinonas/química
Lipoproteínas/química
Lipoproteínas/isolamento & purificação
Thermoplasma/química
[Mh] Termos MeSH secundário: Benzoquinonas/isolamento & purificação
Microscopia Crioeletrônica
Lipídeos/química
Lipídeos/isolamento & purificação
Lipoproteínas/metabolismo
Proteoma
Vitelogeninas/química
Vitelogeninas/genética
Vitelogeninas/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoquinones); 0 (Lipids); 0 (Lipoproteins); 0 (Proteome); 0 (Vitellogenins); 3T006GV98U (quinone)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160714
[St] Status:MEDLINE


  5 / 444 MEDLINE  
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[PMID]:26949259
[Au] Autor:Danev R; Baumeister W
[Ad] Endereço:Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.
[Ti] Título:Cryo-EM single particle analysis with the Volta phase plate.
[So] Source:Elife;5, 2016 Mar 07.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We present a method for in-focus data acquisition with a phase plate that enables near-atomic resolution single particle reconstructions. Accurate focusing is the determining factor for obtaining high quality data. A double-area focusing strategy was implemented in order to achieve the required precision. With this approach we obtained a 3.2 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome. The phase plate matches or slightly exceeds the performance of the conventional defocus approach. Spherical aberration becomes a limiting factor for achieving resolutions below 3 Å with in-focus phase plate images. The phase plate could enable single particle analysis of challenging samples in terms of small size, heterogeneity and flexibility that are difficult to solve by the conventional defocus approach.
[Mh] Termos MeSH primário: Microscopia Crioeletrônica/métodos
Complexo de Endopeptidases do Proteassoma/ultraestrutura
Thermoplasma/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160308
[St] Status:MEDLINE


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[PMID]:26919387
[Au] Autor:Jo CH; Kim J; Han AR; Park SY; Hwang KY; Nam KH
[Ad] Endereço:Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, Korea.
[Ti] Título:Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine.
[So] Source:FEBS Lett;590(6):848-56, 2016 Mar.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Site-specific Xer recombination plays a pivotal role in reshuffling genetic information. Here, we report the 2.5 Å crystal structure of XerA from the archaean Thermoplasma acidophilum. Crystallographic data reveal a uniquely open conformational state, resulting in a C-shaped clamp with an angle of ~ 48° and a distance of 57 Å between the core-binding and the catalytic domains. The catalytic nucleophile, Tyr264, is positioned in cis-cleavage mode by XerA's C-term tail that interacts with the CAT domain of a neighboring monomer without DNA substrate. Structural comparisons of tyrosine recombinases elucidate the dynamics of Xer recombinase.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Proteínas Arqueais/metabolismo
Recombinases/química
Recombinases/metabolismo
Thermoplasma/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas Arqueais/genética
Domínio Catalítico
Cristalografia por Raios X
Genes Arqueais
Modelos Moleculares
Dados de Sequência Molecular
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Recombinases/genética
Homologia de Sequência de Aminoácidos
Eletricidade Estática
Thermoplasma/genética
Tirosina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Recombinant Proteins); 0 (Recombinases); 42HK56048U (Tyrosine)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160323
[Lr] Data última revisão:
160323
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160227
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12109


  7 / 444 MEDLINE  
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[PMID]:26896802
[Au] Autor:Constantinescu-Aruxandei D; Petrovic-Stojanovska B; Penedo JC; White MF; Naismith JH
[Ad] Endereço:Biomedical Sciences Research Complex, University of St Andrews, Fife KY16 9ST, UK.
[Ti] Título:Mechanism of DNA loading by the DNA repair helicase XPD.
[So] Source:Nucleic Acids Res;44(6):2806-15, 2016 Apr 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The xeroderma pigmentosum group D (XPD) helicase is a component of the transcription factor IIH complex in eukaryotes and plays an essential role in DNA repair in the nucleotide excision repair pathway. XPD is a 5' to 3' helicase with an essential iron-sulfur cluster. Structural and biochemical studies of the monomeric archaeal XPD homologues have aided a mechanistic understanding of this important class of helicase, but several important questions remain open. In particular, the mechanism for DNA loading, which is assumed to require large protein conformational change, is not fully understood. Here, DNA binding by the archaeal XPD helicase from Thermoplasma acidophilum has been investigated using a combination of crystallography, cross-linking, modified substrates and biochemical assays. The data are consistent with an initial tight binding of ssDNA to helicase domain 2, followed by transient opening of the interface between the Arch and 4FeS domains, allowing access to a second binding site on helicase domain 1 that directs DNA through the pore. A crystal structure of XPD from Sulfolobus acidocaldiarius that lacks helicase domain 2 has an otherwise unperturbed structure, emphasizing the stability of the interface between the Arch and 4FeS domains in XPD.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Reparo do DNA
DNA Arqueal/química
DNA de Cadeia Simples/química
Thermoplasma/química
Proteína Grupo D do Xeroderma Pigmentoso/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Proteínas Arqueais/antagonistas & inibidores
Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Sítios de Ligação
Clonagem Molecular
Cristalografia por Raios X
Dano ao DNA
DNA Arqueal/genética
DNA Arqueal/metabolismo
DNA de Cadeia Simples/genética
DNA de Cadeia Simples/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Modelos Moleculares
Dados de Sequência Molecular
Ligação Proteica
Estabilidade Proteica
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Sulfolobus/química
Sulfolobus/enzimologia
Thermoplasma/enzimologia
Proteína Grupo D do Xeroderma Pigmentoso/genética
Proteína Grupo D do Xeroderma Pigmentoso/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (DNA, Archaeal); 0 (DNA, Single-Stranded); 0 (Recombinant Proteins); EC 3.6.4.12 (Xeroderma Pigmentosum Group D Protein)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160221
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw102


  8 / 444 MEDLINE  
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[PMID]:26856373
[Au] Autor:Paul DM; Beuron F; Sessions RB; Brancaccio A; Bigotti MG
[Ad] Endereço:School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol BS8 1TD, UK.
[Ti] Título:Internal (His)6-tagging delivers a fully functional hetero-oligomeric class II chaperonin in high yield.
[So] Source:Sci Rep;6:20696, 2016 Feb 09.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Group II chaperonins are ATP-ases indispensable for the folding of many proteins that play a crucial role in Archaea and Eukarya. They display a conserved two-ringed assembly enclosing an internal chamber where newly translated or misfolded polypeptides can fold to their native structure. They are mainly hexadecamers, with each eight-membered ring composed of one or two (in Archaea) or eight (in Eukarya) different subunits. A major recurring problem within group II chaperonin research, especially with the hetero-oligomeric forms, is to establish an efficient recombinant system for the expression of large amounts of wild-type as well as mutated variants. Herein we show how we can produce, in E. coli cells, unprecedented amounts of correctly assembled and active αß-thermosome, the class II chaperonin from Thermoplasma acidophilum, by introducing a (His)6-tag within a loop in the α subunit of the complex. The specific location was identified via a rational approach and proved not to disturb the structure of the chaperonin, as demonstrated by size-exclusion chromatography, native gel electrophoresis and electron microscopy. Likewise, the tagged protein showed an ATP-ase activity and an ability to refold substrates identical to the wild type. This tagging strategy might be employed for the overexpression of other recombinant chaperonins.
[Mh] Termos MeSH primário: Proteínas Arqueais
Chaperoninas do Grupo II
Histidina
Proteínas Recombinantes de Fusão
Thermoplasma/genética
[Mh] Termos MeSH secundário: Proteínas Arqueais/biossíntese
Proteínas Arqueais/genética
Chaperoninas do Grupo II/biossíntese
Chaperoninas do Grupo II/genética
Histidina/biossíntese
Histidina/genética
Proteínas Recombinantes de Fusão/biossíntese
Proteínas Recombinantes de Fusão/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Recombinant Fusion Proteins); 26062-48-6 (polyhistidine); 4QD397987E (Histidine); EC 3.6.1.- (Group II Chaperonins)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160210
[St] Status:MEDLINE
[do] DOI:10.1038/srep20696


  9 / 444 MEDLINE  
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[PMID]:26825464
[Au] Autor:Rohleder F; Huang J; Xue Y; Kuper J; Round A; Seidman M; Wang W; Kisker C
[Ad] Endereço:Rudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Würzburg, D-97080 Würzburg, Germany.
[Ti] Título:FANCM interacts with PCNA to promote replication traverse of DNA interstrand crosslinks.
[So] Source:Nucleic Acids Res;44(7):3219-32, 2016 Apr 20.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:FANCM is a highly conserved DNA remodeling enzyme that promotes the activation of the Fanconi anemia DNA repair pathway and facilitates replication traverse of DNA interstrand crosslinks. However, how FANCM interacts with the replication machinery to promote traverse remains unclear. Here, we show that FANCM and its archaeal homolog Hef from Thermoplasma acidophilum interact with proliferating cell nuclear antigen (PCNA), an essential co-factor for DNA polymerases in both replication and repair. The interaction is mediated through a conserved PIP-box; and in human FANCM, it is strongly stimulated by replication stress. A FANCM variant carrying a mutation in the PIP-box is defective in promoting replication traverse of interstrand crosslinks and is also inefficient in promoting FANCD2 monoubiquitination, a key step of the Fanconi anemia pathway. Our data reveal a conserved interaction mode between FANCM and PCNA during replication stress, and suggest that this interaction is essential for FANCM to aid replication machines to traverse DNA interstrand crosslinks prior to post-replication repair.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Proteínas Arqueais/metabolismo
DNA Helicases/química
DNA Helicases/metabolismo
Reparo do DNA
Replicação do DNA
Antígeno Nuclear de Célula em Proliferação/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sequência de Aminoácidos
Sítios de Ligação
Sequência Conservada
DNA Helicases/genética
Seres Humanos
Modelos Moleculares
Mutação
Estresse Fisiológico
Thermoplasma/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Proliferating Cell Nuclear Antigen); EC 3.6.1.- (FANCM protein, human); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160131
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw037


  10 / 444 MEDLINE  
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[PMID]:26721388
[Au] Autor:Kawamura T; Hirata A; Ohno S; Nomura Y; Nagano T; Nameki N; Yokogawa T; Hori H
[Ad] Endereço:Department of Materials Science and Biotechnology, Graduate School of Science and Engineering, Ehime University, Bunkyo 3, Matsuyama, Ehime 790-8577, Japan.
[Ti] Título:Multisite-specific archaeosine tRNA-guanine transglycosylase (ArcTGT) from Thermoplasma acidophilum, a thermo-acidophilic archaeon.
[So] Source:Nucleic Acids Res;44(4):1894-908, 2016 Feb 29.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Archaeosine (G(+)), which is found only at position 15 in many archaeal tRNA, is formed by two steps, the replacement of the guanine base with preQ0 by archaeosine tRNA-guanine transglycosylase (ArcTGT) and the subsequent modification of preQ0 to G(+) by archaeosine synthase. However, tRNA(Leu) from Thermoplasma acidophilum, a thermo-acidophilic archaeon, exceptionally has two G(+)13 and G(+)15 modifications. In this study, we focused on the biosynthesis mechanism of G(+)13 and G(+)15 modifications in this tRNA(Leu). Purified ArcTGT from Pyrococcus horikoshii, for which the tRNA recognition mechanism and structure were previously characterized, exchanged only the G15 base in a tRNA(Leu) transcript with (14)C-guanine. In contrast, T. acidophilum cell extract exchanged both G13 and G15 bases. Because T. acidophilum ArcTGT could not be expressed as a soluble protein in Escherichia coli, we employed an expression system using another thermophilic archaeon, Thermococcus kodakarensis. The arcTGT gene in T. kodakarensis was disrupted, complemented with the T. acidophilum arcTGT gene, and tRNA(Leu) variants were expressed. Mass spectrometry analysis of purified tRNA(Leu) variants revealed the modifications of G(+)13 and G(+)15 in the wild-type tRNA(Leu). Thus, T. acidophilum ArcTGT has a multisite specificity and is responsible for the formation of both G(+)13 and G(+)15 modifications.
[Mh] Termos MeSH primário: Glicosídeo Hidrolases/genética
Complexos Multienzimáticos/genética
RNA de Transferência/genética
Thermoplasma/enzimologia
Transferases/genética
[Mh] Termos MeSH secundário: Regulação Enzimológica da Expressão Gênica
Glicosídeo Hidrolases/química
Glicosídeo Hidrolases/metabolismo
Complexos Multienzimáticos/química
Complexos Multienzimáticos/metabolismo
Pyrococcus horikoshii/enzimologia
Thermoplasma/genética
Transferases/química
Transferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Multienzyme Complexes); 0 (transglycosidase enzyme system); 9014-25-9 (RNA, Transfer); EC 2.- (Transferases); EC 3.2.1.- (Glycoside Hydrolases)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160102
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkv1522



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