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The human Tim-Tipin complex interacts directly with DNA polymerase epsilon and stimulates its synthetic activity.

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.

SUBMITTER: Aria V 

PROVIDER: S-EPMC3642320 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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The human Tim-Tipin complex interacts directly with DNA polymerase epsilon and stimulates its synthetic activity.

Aria Valentina V   De Felice Mariarita M   Di Perna Roberta R   Uno Shuji S   Masai Hisao H   Syväoja Juhani E JE   van Loon Barbara B   Hübscher Ulrich U   Pisani Francesca M FM  

The Journal of biological chemistry 20130319 18

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 ε. In contrast, no significant effect on the synthetic ability of human DNA polymerase α and δ by Tim-Tipin was observed. Surface plasmon resonance meas  ...[more]

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