Communicating across the membrane during bacterial cell division (Newcastle)

The activities of various processes need to be co-ordinated during bacterial cell division. One such example is the way that the constriction of the division septum – driven by the cytoplasmic tubulin homolog, FtsZ – is linked to the synthesis of new peptidoglycan, which is deposited on the extracellular face of the membrane at the division site. Peptidoglycan synthesis is targeted by penicillin and vancomycin, some of mankind’s most widely-used antibiotics, however the increasing threat to human health of antimicrobial resistance means that alternative targets need to be identified. We are particularly interested in how cell division regulators link FtsZ dynamics to peptidoglycan synthesis catalysed by PBP1. Interestingly, the catalytic apparatus of PBP1 is located on the outside face of the cell yet most of the regulators we will study are found on the inside of the cell; it is simply not known how these interactions affects PBP1 function. We will capitalize on our recent structure determination of two important regulators to interrogate how proteins in the cytoplasm affect the properties of enzymes whose active sites are outside the cell, and whether these interactions can be exploited in the future. The procedures adopted for the study will include the biochemistry of peptidoglycan synthesis, the biophysics of protein:protein interactions and X-ray crystallography. The supervisory team are world-leading experts in the application of these techniques to the problem of how bacteria build their outer defensive envelopes and how the synthesis of these envelopes is targeted by antimicrobials.

For further information see the website: http://www.ncl.ac.uk/camb/

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