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Structural and functional studies of outer membrane assembly in Gram-negative bacteria and mitochondria - DongMED_Oct2020


Project Description

The outer membrane plays essential roles in Gram-negative bacteria and mitochondria. Dysfunction of outer membrane proteins occur in several human diseases, such as diabetes, Parkinson and other neurodegenerative disease. In Gram-negative bacteria, BAM machinery is responsible for outer membrane biogenesis, while the SAM complex in mitochondria inserts and folds membrane proteins into the outer membrane. This project is an exciting and timely opportunity to carry out structural and functional studies of BAM complexes with different substrates using multi-discipline approaches, covering structural biology, biochemistry, microbiology, cell biology and molecular biology.

Following on from our successful work on the BAM complex, this project will focus on the structural mechanisms of outer membrane protein recognition, transport and insertion by BAM complexes, which will help us to understand mitochondrial outer membrane biogenesis and function. The research will include gene cloning, protein expression, protein purification, protein complex crystallization, cryo-EM, structural determination, mutagenesis and cell-based assays.

The successful candidate will work in Prof. Changjiang Dong’s and Dr. Paul Crichton’s Labs at the Biomedical Research Centre, which are equipped with state-of-the-art instruments. Here, they will benefit from an excellent scientific research environment with great opportunities for collaboration and training across the Norwich Research Park.

More information on the supervisor for this project: https://people.uea.ac.uk/c_dong

Type of programme: PhD
Start date: October 2020
Mode of study: Full-time
Studentship length: 3 years

Funding Notes

This PhD project is in a Faculty of Medicine and Health Sciences competition for funded studentships. These studentships are funded for 3 years and comprise of Home/EU fees, a stipend of £15,009 and £1000 per annum to support research training.

References

i) Gu Y, Li H, Dong H, Zeng Y, Zhang Z, Paterson NG, Stansfeld PJ, Wang Z, Zhang Y, Wang W, Dong C. Structural basis of outer membrane protein insertion by the BAM complex Nature. 2016 Mar 3;531(7592):64-9. doi: 10.1038/nature17199.
ii) Dong H, Xiang Q, Gu Y, Wang Z, Paterson NG, Stansfeld PJ, He C, Zhang Y, Wang W, Dong C. (2014) Structural basis for outer membrane lipopolysaccharide insertion. Nature. 511:52-6. doi: 10.1038/nature13464.
iii) Dong H, Zhang Z, Tang X, Paterson NG, Dong C.Structural and functional insights into the lipopolysaccharide ABC transporter LptB2FG. Nat Commun. 2017 Aug 9;8(1):222. doi: 10.1038/s41467-017-00273-5.
iv) Tang X, Chang S, Luo Q, Zhang Z, Qiao W, Xu C, Zhang C, Niu Y, Yang W, Wang T, Zhang Z, Zhu X, Wei X, Dong C, Zhang X, Dong H. Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism. Nat Commun. 2019 Sep 13;10(1):4175. doi: 10.1038/s41467-019-11977-1.
v) Ruprecht JJ, King MS, Zögg T, Aleksandrova AA, Pardon E, Crichton PG, Steyaert J, Kunji ERS.The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier.Cell. 2019 Jan 24;176(3):435-447.e15. doi: 10.1016/j.cell.2018.11.025. Epub 2019 Jan 2.

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