This is an ideal opportunity for an enthusiastic and creative scientist to join a dynamic research team with excellent collaborators and facilities. The successful applicant will use cutting-edge biochemical approaches to work on a high profile project investigating novel mechanisms in eukaryotic DNA replication with therapeutic potential. The project will address: how do key DNA replication factors function and how they are regulated....
Job listing information
- Reference MED01085
- Date posted 19 February 2019
- Closing date 25 March 2019
This is an ideal opportunity for an enthusiastic and creative scientist to join a dynamic research team with excellent collaborators and facilities. The successful applicant will use cutting-edge biochemical approaches to work on a high profile project investigating novel mechanisms in eukaryotic DNA replication with therapeutic potential.
The project will address: how do key DNA replication factors function and how they are regulated. This type of work is crucial to understand how cancer development is initiated and will serve as a stepping-stone for the future development of replication inhibitors with potential as chemotherapeutic drugs. The successful candidate will take advantage of efficient and well-established reconstituted systems and in vivo approaches (Evrin et al PNAS 2009, Fernandez-Cid et al Mol Cell 2013, Sun et al NSMB 2013, Samel et al G&D 2014, Sun et al G&D 2014, Chang et al 2015 Elife, Noguchi et al PNAS 2017) to address how the replicative helicase becomes loaded onto DNA. It is the ideal time point to start with this project, as a recent high resolution structure of the replicative helicase in complex with its loader by the Speck lab (Yuan et al NSMB 2017) has helped the group to formulate a number of new hypotheses. The main aim of the project is to discover how Cdt1 functions in MCM2-7 ring opening/closing and induction of ATP-hydrolysis, two key events during initiation of DNA replication. The research will involve design of constructs, expression and purification of proteins & protein complexes using bacteria and yeast. The purified factors will be used in established and novel biochemical assays (see Fernandez-Cid et al Mol Cell 2013), while structural analysis and analysis of protein dynamics by FRET assays will be carried out in collaboration with other group members and an local collaborator. The applicant will be working as part of a team, and will have ample opportunity to drive the project’s direction in a creative way.
Duties and responsibilities
The successful candidate will enjoy intensive interactions with group members specialised in cryo-EM, biochemistry or in vivo approaches generating a collaborative and highly productive atmosphere, with opportunities for advanced training. The lab is excellent equipped for biochemistry (2 AKTA’s, 4 temperature controlled shakers, 2 freezer mills, constant system french press, Biacore T100), structural EM work and has direct access to a staffed local cryo-EM facility (200kV FEG cryo-EM, Vitrobot IV, GPU- and data storage-cluster) and the Titan Krios as founding member of the LonCEN consortium.
By joining the group, the candidate will not only participate in high profile research projects, but will be also directly mentored by Professor Speck in grant writing, networking and publishing. Indeed, the scientific framework and the support by Prof. Speck means that the candidate is well placed for a successful transition into independence.
The candidate should have a PhD in Biochemistry or neighbouring disciplines, a strong publication record and extensive expertise in protein biochemistry and biochemical assays. Background in the areas of nucleic acid-protein interactions, molecular machines, or the broader area of genome stability would be of advantage, but is not necessary.
The position is available right away and the latest expected start date is middle 2019.
For informal inquiries or questions please contact Professor Christian Speck directly (email@example.com).
For technical issues when applying online please email firstname.lastname@example.org
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