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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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| 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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