http://www.cnr.it/ontology/cnr/individuo/prodotto/ID245466
The physical interaction of Mcm10 with Cdc45 modulates their DNA binding properties. (Articolo in rivista)
- Type
- Label
- The physical interaction of Mcm10 with Cdc45 modulates their DNA binding properties. (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1042/BJ20130059 (literal)
- Alternative label
Di Perna R, Aria V, De Falco M, Sannino V, Okorokov AL, Pisani FM, De Felice M (2013)
The physical interaction of Mcm10 with Cdc45 modulates their DNA binding properties.
in Biochemical journal (Online)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Di Perna R, Aria V, De Falco M, Sannino V, Okorokov AL, Pisani FM, De Felice M (literal)
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Biochimica delle Proteine - CNR (literal)
- Titolo
- The physical interaction of Mcm10 with Cdc45 modulates their DNA binding properties. (literal)
- Abstract
- The Tim-Tipin complex plays an important role in the S phase checkpoint and replication fork stability in metazoans, but the molecular mechanism underlying its biological function is poorly understood. Here, we present evidence that the recombinant human Tim-Tipin complex (and Tim alone) markedly enhances the synthetic activity of DNA polymerase ?. In contrast, no significant effect on the synthetic ability of human DNA polymerase ? and ? by Tim-Tipin was observed. Surface plasmon resonance measurements and co-immunoprecipitation experiments revealed that recombinant DNA polymerase ? directly interacts with either Tim or Tipin. In addition, the results of DNA band shift assays suggest that the Tim-Tipin complex (or Tim alone) is able to associate with DNA polymerase ? bound to a 40-/80-mer DNA ligand. Our results are discussed in view of the molecular dynamics at the human DNA replication fork. (literal)
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