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Determination of the molecular architectures of centrosomes and basal bodies using a novel labelling method and cryo-electron tomography


Project Description

This project is to determine exact locations of centrosomal and ciliary proteins by developing antibody-like proteins that can specifically recognise targets and by using cryo-electron microscopy.

Centrosomes play central roles in cell division by nucleating microtubules that equally divide duplicated chromosomes into two dividing cells. In addition, centrosomes are essential for generating cilia because the core structure of the centrosome becomes the base of the cilium. Since centrosomes and cilia are highly-ordered protein complexes, they must maintain correct architectures for their normal functions. Indeed, mutations on many centrosomal and ciliary genes cause abnormal development due to their structure defects. Therefore, understanding how each protein contributes to build these organelles is important. However, we know little about exact contributions of most of centrosomal and ciliary proteins to their structures. To resolve this problem, my group currently focuses on determining the structure that is shared between the centrosome and cilium.

During the project, the successful candidate will use bacterial, insect and human cells for protein, production, purification and characterisation. Also, the student will learn how to use our state-of-art cryo-electron microscopes and analyse their data.

Funding Notes

White Rose BBSRC Doctoral Training Partnership in Mechanistic Biology
4 year fully-funded programme of integrated research and skills training, starting Oct 2019:
• Research Council Stipend
• UK/EU Tuition Fees
• Conference allowance
• Research Costs

Requirements:
At least a 2:1 honours degree or equivalent. We welcome students with backgrounds in biological, chemical or physical sciences, or mathematical backgrounds with an interest in biological questions.
EU candidates require 3 years of UK residency in order to receive full studentship

Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process.

View Website

References

Ochi laboratory: https://ochilab.org
Tomlinson laboratory: http://dctomlinson.wixsite.com/laboratory

Tiede C, Bedford R, Heseltine SJ, Smith G, Wijetunga I, Ross R, AlQallaf D, Roberts AP, Balls A, Curd A, Hughes RE, Martin H, Needham SR, Zanetti-Domingues LC, Sadigh Y, Peacock TP, Tang AA, Gibson N, Kyle H, Platt GW, Ingram N, Taylor T, Coletta LP, Manfield I, Knowles M, Bell S, Esteves F, Maqbool A, Prasad RK, Drinkhill M, Bon RS, Patel V, Goodchild SA, Martin-Fernandez M, Owens RJ, Nettleship JE, Webb ME, Harrison M, Lippiat JD, Ponnambalam S, Peckham M, Smith A, Ferrigno PK, Johnson M, McPherson MJ, Tomlinson DC*. Affimer proteins are versatile and renewable affinity reagents.  Elife. 2017 Jun 27;6. pii: e24903. doi: 10.7554/eLife.24903

Robinson JI, Baxter E, Owen RL, Thomsen M, Tomlinson DC, Waterhouse MP, Win SJ, Nettleship JE, Tiede C, Foster RJ, Owens RJ, Fishwick CWG, Harris SA, Goldman A, McPherson MJ, Morgan AW. Affimers inhibit immune complex binding to FcgRIIIa with high specificity through competitive and allosteric modes of action. Proc Natl Acad Sci U S A. 2018 Jan 2;115(1):E72-E81. doi: 10.1073/pnas.1707856115

How good is research at University of Leeds in Biological Sciences?

FTE Category A staff submitted: 60.90

Research output data provided by the Research Excellence Framework (REF)

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