Tag - DNA replication

VACANCY: Research associate x 2 in biochemistry and structural biology (MED02737)

Reference: MED02737 Date posted: 21 September 2021 Closing date: 19 October 2021 Two full-time research associate positions are available to investigate mechanisms of human DNA replication and their misregulation in cancer employing biochemical and structural or genomic approaches, with the aim of discovering how DNA replication origins are specified (position 1), and how DNA replication is regulated (position 2), to support genome stability and achieve faithful DNA replication. Position 1 requires expertise in biochemistry, while position 2 in cryo-EM. Job details | Apply

VACANCY: Research associate in genomics (MED02738)

Reference: MED02738 Date posted: 21 September 2021 Closing date: 19 October 2021 A full-time research associate is available to investigate mechanisms of human DNA replication and their misregulation in cancer employing biochemical and structural or genomic approaches. The successful applicant will employ high resolution genomics (ChIP-Exo or CUT&RUN), proteomic (ChIP-MS) and cell biological approaches to discover novel mechanisms in the function of human DNA replication origins and explore how misregulation of replication origins leads to genomic instability. Expertise in high-resolution genomics and bioinformatic analysis of data is essential. Job details | Apply

New paper on the molecular mechanism in the licensing of eukaryotic replication origins

Feng, X., Noguchi, Y., Barbon, M., Stillman, B., Speck, C., Li, H. (2021). The structure of ORC-Cdc6 on an origin DNA reveals the mechanism of ORC activation by the replication initiator Cdc6. Nature Communications 12, 3883. Abstract | Full Text |

New paper on the structural mechanism of helicase loading

Yuan, Z., Schneider, S., Dodd, T., Riera, A., Bai, L., Yan, C., Magdalou, I., Ivanov, I., Stillman, B., Li, H., Speck, C. (2020). Structural mechanism of helicase loading onto replication origin DNA by ORC-Cdc6. Proceedings of the National Academy of Sciences of the United States of America 117, 17747-17756. Abstract | Full Text |

New paper proposes lagging-strand DNA extrusion mechanism

Noguchi, Y., Yuan, Z., Bai, L., Schneider, S., Zhao, G., Stillman, B., Speck, C., Li, H. (2017). Cryo-EM structure of Mcm2-7 double hexamer on DNA suggests a lagging-strand DNA extrusion model. Proceedings of the National Academy of Sciences of the United States of America 114, E9529-E9538. Abstract | Full text |

New paper shows Cdc6 ATPase activity promotes DNA replication

Chang, F., Riera, A., Evrin, C., Sun, J., Li, H., Speck, C., Weinreich, M. (2015). Cdc6 ATPase activity disengages Cdc6 from the pre-replicative complex to promote DNA replication. eLife 4, e05759.
Abstract | Full text | Biomedical Picture of the Day | MRC Clinical Sciences Centre News | Imperial College London News |

New paper on regulation of loading of MCM2-7 onto DNA

Samel, S. A., Fernández-Cid, A., Sun, J., Riera, A., Tognetti, S., Herrera, C., Li, H., Speck, C. (2014). A unique DNA entry gate serves for regulated loading of the eukaryotic replicative helicase MCM2–7 onto DNA. Genes & Development 28, 1653-1666.
Abstract | Imperial College London News |