12Nov2020
Project title: Developing advanced mass photometry methods for analysis of the multi-step helicase loading process
Lead supervisor: Christian Speck
Funding: EPSRC
Start date: October 2021
Duration: 3.5 years
Date posted: 12 November 2020
Closing date: 07 January 2021
The student will use and develop a novel single-molecule biophysical method (mass photometry) to investigate a key step in DNA replication, the loading of the replicative helicase on DNA, and explore this multi-step reaction in a time resolved manner. This work will address how DNA replication works and contribute to the development of helicase loading inhibitors as a potential anti-cancer therapy.
The project is a collaboration between Refeyn Ltd and the Imperial College London research groups of Christian Speck and David Rueda. Refeyn, a company based in Oxford, has recently developed and brought to market a breakthrough technology that measures the molecular weight of individual proteins and protein complexes by mass photometry. This revolutionary biophysical technique is highly-accurate, very fast, label-free and allows the use of native proteins.
The group of Christian Speck, which includes seven postdocs, three PhD students and two technicians, applies a range of biochemical, structural, proteomic and genetic/genomic approaches in order to investigate DNA replication and chromatin structure. The Group works in a highly collaborative way and provides PhD students with a multidisciplinary learning environment. Applicants that interested in genome stability and method development and have a good background in biochemistry or biophysics are strongly encouraged to apply.
Interested candidates can contact Christian Speck directly for more information.
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15Jul2020
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 |
07Nov2019
Group awarded BBSRC project grant
The Group's Biotechnology and Biological Sciences Research Council (BBSRC) grant application was successful! Huge congratulations to Sarah Schneider, Almutasem Saleh and Yasunori Noguchi for writing a fantastic proposal and achieving a superb ranking of fourth out of 89. Two new postdoctoral positions will open soon. Interested candidates should contact Christian Speck.
11Oct2019
Data collected using new Titan Krios cryo-EM
First data collected using the London Consortium for cryo-EM's (LonCEM's) new Titan Krios Cryo Transmission Electron Microscope with the Gatan K3™ camera in super-resolution mode. A dream come true.
25Oct2017
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 |
06Jul2017
Katalin Kondas participates in EMBO Practical Course
As a selected participant, Katalin Kondas attends the EMBO Practical Course "High-throughput protein production and crystallization”, 6 – 14 July 2017 in Harwell, Oxfordshire, UK.
01Jun2017
13Feb2017
29Sep2016
Henry Gerdes defends MSc thesis
Henry Gerdes passes his MSc viva with distinction. Congratulations and well done Henry!
17Jul2016
New article commentary on Cdc45 overexpression
Speck, C. (2016). Exceeding the limits – Cdc45 overexpression turns bad. Cell Cycle 15, 1809-1810.
Full text |
27May2016
New article about replicating repetitive DNA
Tognetti, S., Speck, C. (2016). Replicating repetitive DNA. Nature Cell Biology 18, 593-594.
Abstract |
03Sep2015
New paper on assembly of the eukaryotic replicative helicase
Herrera, M. C.*, Tognetti, S.*, Riera, A., Zech, J., Clarke, P., Fernández-Cid, A., Speck, C. (2015). A reconstituted system reveals how activating and inhibitory interactions control DDK dependent assembly of the eukaryotic replicative helicase. Nucleic Acids Research 43, 10238-10250.
*Shared first authorship
Abstract | Full text |