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Registros recuperados: 11
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Binding to PCNA in Euryarchaeal DNA Replication Requires Two PIP Motifs for DNA Polymerase D and One PIP Motif for DNA Polymerase B ArchiMer
Castrec, Benoit; Rouillon, Christophe; Henneke, Ghislaine; Flament, Didier; Querellou, Joel; Raffin, Jean-paul.
Replicative DNA polymerases possess a canonical C-terminal proliferating cell nuclear antigen (PCNA)-binding motif termed the PCNA-interacting protein (PIP) box. We investigated the role of the PIP box on the functional interactions of the two DNA polymerases, PabPol B (family B) and PabPol D (family D), from the hyperthermophilic euryarchaeon Pyrococcus abyssi, with its cognate PCNA. The PIP box was essential for interactions of PabPol B with PCNA, as shown by surface plasmon resonance and primer extension studies. In contrast, binding of PabPol D to PCNA was affected only partially by removing the PIP motif. We identified a second palindromic PIP box motif at the N-terminus of the large subunit of PabPol D that was required for the interactions of PabPol...
Tipo: Text Palavras-chave: Archaea; PIP box; PCNA binding motifs; DNA polymerases; DNA replication.
Ano: 2009 URL: http://archimer.ifremer.fr/doc/2009/publication-7317.pdf
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DNA polymerase switching on homotrimeric PCNA at the replication fork of the euryarchaea Pyrococcus abyssi ArchiMer
Rouillon, Christophe; Henneke, Ghislaine; Flament, Didier; Querellou, Joel; Raffin, Jean-paul.
DNA replication in Archaea, as in other organisms, involves large protein complexes called replisomes. In the Euryarchaeota subdomain, only two putative replicases have been identified, and their roles in leading and lagging strand DNA synthesis are still poorly understood. In this study, we focused on the coupling of proliferating cell nuclear antigen (PCNA)loading mechanisms with DNA polymerase function in the Euryarchaea Pyrococcus abyssi. PCNA spontaneously loaded onto primed DNA, and replication factor C dramatically increased this loading. Surprisingly, the family B DNA polymerase (Pol B) also increased PCNA loading, probably by stabilizing the clamp on primed DNA via an essential motif. In contrast, on an RNA-primed DNA template, the PCNA/Pol B...
Tipo: Text Palavras-chave: RF C; PCNA loading; DNA polymerase switching; DNA replication; Archaea.
Ano: 2007 URL: http://archimer.ifremer.fr/doc/2007/publication-2638.pdf
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DNA replication stress: oncogenes in the spotlight Genet. Mol. Biol.
Primo,Luiza M. F.; Teixeira,Leonardo K..
Abstract Precise replication of genetic material is essential to maintain genome stability. DNA replication is a tightly regulated process that ensues faithful copies of DNA molecules to daughter cells during each cell cycle. Perturbation of DNA replication may compromise the transmission of genetic information, leading to DNA damage, mutations, and chromosomal rearrangements. DNA replication stress, also referred to as DNA replicative stress, is defined as the slowing or stalling of replication fork progression during DNA synthesis as a result of different insults. Oncogene activation, one hallmark of cancer, is able to disturb numerous cellular processes, including DNA replication. In fact, extensive work has indicated that oncogene-induced replication...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Cancer; Cell cycle; DNA replication; Oncogene; Replication stress.
Ano: 2020 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572020000200301
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Interactions entre composants de la maintenance génomique chez les Archaea hyperthermophiles: Étude des associations entre PCNA et le complexe Mre11-Rad50 et entre les hélicases MCM et XPD ArchiMer
Hogrel, Gaëlle.
Living at temperatures above 80°C, hyperthermophilic Archaea demonstrated amazing capacity to recover from DNA damages, suggesting they arguably have efficient genome guardians. These guardians, proteins which are relatively similar between Archaea and eukaryotes, act and interact like a ballet orchestrated by the cell. Several proteins involved in essential repair pathway in eukaryotes are missing in Archaea. To gain insights into archaeal genome maintenance processes, a previous work proposed a protein-protein interaction network based on Pyrococcus abyssi proteins. Through this network, new interactions involving proteins from DNA replication and proteins from DNA repair were highlighted. To describe interactions for a better understanding of their...
Tipo: Text Palavras-chave: Archée; Réplication et Recombinaison de l’ADN; Interaction protéine-protéine.; Archaea; DNA replication; DNA repair & recombination; Protein-protein interaction..
Ano: 2015 URL: http://archimer.ifremer.fr/doc/00300/41158/40351.pdf
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La réplication de l'ADN chez l'euryarchaea Pyrococcus Abyssi : mise en place et dynamique du complexe ArchiMer
Rouillon, Christophe.
DNA replication occurs through a large protein complex assembly called replisome. An understanding of its structure and function requires its in vitro reassembly from individual subunits. In all living organisms, the elongation of a primed DNA template by DNA polymerase, with high processivity, requires the accessory protein DNA sliding clamp (PCNA) that is loaded onto DNA by the clamp loader (RF-C). Generally, the archaeal proteins involved in DNA replication are more similar to those of the higher organisms (Eukarya) rather than to those from Bacteria. This study have focussed on the PCNA loading mechanism and on the DNA synthesis in the hyperthermophilic Euryarchaea Pyrococcus abyssi. To investigate the importance of some protein-protein and...
Tipo: Text Palavras-chave: Pyrococcus; Archaea; DNA synthesis; Interaction; RP A; RF C; PCNA; DNA polymerase; DNA replication; Pyrococcus; Archée; Archaea; Synthese d'ADN; Interaction; RP A; RF C; PCNA; ADN polymerase; Replication de l'ADN.
Ano: 2006 URL: http://archimer.ifremer.fr/doc/2006/these-2461.pdf
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Les ADN polymérases B et D de l'Archaea hyperthermophile, Pyrococcus abyssi : contribution à l'étude des relations structure-fonction ArchiMer
Castrec, Benoit.
DNA replication is a functionally conserved mechanism among the three domains of life. This processus is performed by DNA polymerases with two accessories factors, PCNA and RF-C, sliding clamp and clamp loader, respectively. Our model of study, the Euryarchaeota Pyrococcus abyssi, possesses one monomeric DNA polymerase, belonging to the Family B, and one heterodimeric DNA polymerase, belonging to the Family D. Usually, proteins interact with PCNA at a hydrophobic pocket which is formed by the IDCL (interdomain connecting loop) and the C-terminus. These interactions are mediated through common motifs like the PIP box (motif PCNA interacting Protein). We have demonstrated that Pol B has just one PIP box motif at the C-terminus, while Pol D has two PIP-type...
Tipo: Text Palavras-chave: Thermostability; Interactions; Motifs; DNA replication; RF C; PCNA; DNA polymerases; Archaea; Thermostabilité; Interactions; Motifs; Réplication de l'ADN; RF C; PCNA; ADN polymérases; Archaea.
Ano: 2009 URL: http://archimer.ifremer.fr/doc/2009/these-6940.pdf
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Prediction of mutations on structure primase of the archaeon Sulfolobus solfataricus Biological Sciences
Souza, Eden Silva e; Diniz, Michely Correia.
 All living organisms need a DNA replication mechanism and it has been conserved in the three domains of life throughout evolutionary process. Primase is the enzyme responsible for synthesizing de novo RNA primers in DNA replication. Archaeo-Eukaryotic Primase (AEP) is the superfamily that typically forms a heterodimeric complex containing both a small catalytic subunit (PriS) and a large accessory noncatalytic subunit (PriL). Sulfolobus solfataricus is a model organism for research on the Genetics field. The aim of this work was to evaluate, via Bioinformatics tools, three mutations in the large subunit (PriL) of the archaeon Sulfolobus solfataricus. The aspartic acid residue in the positions (Asp) 62, (Asp) 235, (Asp) 241 have been substituted by...
Tipo: Info:eu-repo/semantics/article Palavras-chave: 2.00.00.00-6; 2.02.02.00-8 in silico; PriL; 3D structure; DNA replication; Primer; Mutations. Genética Molecular e de Microorganismos.
Ano: 2017 URL: http://periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/34600
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Replicating animal mitochondrial DNA Genet. Mol. Biol.
McKinney,Emily A.; Oliveira,Marcos T..
The field of mitochondrial DNA (mtDNA) replication has been experiencing incredible progress in recent years, and yet little is certain about the mechanism(s) used by animal cells to replicate this plasmid-like genome. The long-standing strand-displacement model of mammalian mtDNA replication (for which single-stranded DNA intermediates are a hallmark) has been intensively challenged by a new set of data, which suggests that replication proceeds via coupled leading-and lagging-strand synthesis (resembling bacterial genome replication) and/or via long stretches of RNA intermediates laid on the mtDNA lagging-strand (the so called RITOLS). The set of proteins required for mtDNA replication is small and includes the catalytic and accessory subunits of DNA...
Tipo: Info:eu-repo/semantics/article Palavras-chave: DNA replication; Mitochondria; MtSSB; Pol γ; Twinkle.
Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572013000300002
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Roles of the mitochondrial replisome in mitochondrial DNA deletion formation Genet. Mol. Biol.
Oliveira,Marcos T.; Pontes,Carolina de Bovi; Ciesielski,Grzegorz L..
Abstract Mitochondrial DNA (mtDNA) deletions are a common cause of human mitochondrial diseases. Mutations in the genes encoding components of the mitochondrial replisome, such as DNA polymerase gamma (Pol γ) and the mtDNA helicase Twinkle, have been associated with the accumulation of such deletions and the development of pathological conditions in humans. Recently, we demonstrated that changes in the level of wild-type Twinkle promote mtDNA deletions, which implies that not only mutations in, but also dysregulation of the stoichiometry between the replisome components is potentially pathogenic. The mechanism(s) by which alterations to the replisome function generate mtDNA deletions is(are) currently under debate. It is commonly accepted that stalling of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Mitochondria; DNA replication; Human diseases; Pol γ; Twinkle.
Ano: 2020 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572020000200307
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The heterodimeric primase from the euryarchaeon Pyrococcus abyssi: A multifunctional enzyme for initiation and repair? ArchiMer
Le Breton, Magali; Henneke, Ghislaine; Norais, C; Flament, Didier; Myllykallio, H; Querellou, Joel; Raffin, Jean-paul.
We report on the characterization of the DNA primase complex of the hyperthermophilic archaeon Pyrococcus abyssi (Pab). The Pab DNA primase complex is composed of the proteins Pabp41 and Pabp46, which show sequence similarities to the p49 and p58 subunits, respectively, of the eukaryotic polymerase alpha-primase complex. Both subunits were expressed, purified, and characterized. The Pabp41 subunit alone had no RNA synthesis activity but could synthesize long (up to 3 kb) DNA strands. Addition of the Pabp46 subunit increased the rate of DNA synthesis but decreased the length of the DNA fragments synthesized and conferred RNA synthesis capability. Moreover, in our experimental conditions, Pab DNA primase had comparable affinities for ribonucleotides and...
Tipo: Text Palavras-chave: Strand displacement; Gap filling; DNA primase; Archaea; DNA replication.
Ano: 2007 URL: http://archimer.ifremer.fr/doc/2007/publication-3520.pdf
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The hyperthermophilic euryarchaeota Pyrococcus abyssi likely requires the two DNA polymerases D and B for DNA replication ArchiMer
Henneke, Ghislaine; Flament, Didier; Hubscher, Ulrich; Querellou, Joel; Raffin, Jean-paul.
DNA polymerases carry out DNA synthesis during DNA replication, DNA recombination and DNA repair. During the past five years, the number of DNA polymerases in both eukarya and bacteria has increased to at least 19 and multiple biological roles have been assigned to many DNA polymerases. Archaea, the third domain of life, on the other hand, have only a subset of the eukaryotic-like DNA polymerases. The diversity among the archaeal DNA polymerases poses the intriguing question of their functional tasks. Here, we focus on the two identified DNA polymerases, the family B DNA polymerase B (PabpolB) and the family D DNA polymerase D (PabpolD) from the hyperthermophilic euryarchaeota Pyrococcus abyssi. Our data can be summarized as follows: (i) both Pabpols are...
Tipo: Text Palavras-chave: DNA polymerase; Strand displacement; Gap filling; Euryarchaea; DNA replication.
Ano: 2005 URL: http://archimer.ifremer.fr/doc/2005/publication-423.pdf
Registros recuperados: 11
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