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| 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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| 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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