Cheryl Woolhead
Senior Lecturer
Department of Molecular, Cell and Systems Biology
University of Glasgow
United Kingdom
Biography
Cheryl Woolhead is currently working as a Senior Lecturer in the Department of Molecular, Cell and Systems Biology
Research Interest
Membrane protein folding and insertion Inner membrane proteins make up 20-30% of the bacterial proteome. The major route of insertion for such proteins is via the Sec machinery. However certain membrane proteins are Sec independent and instead insert via an essential membrane protein called YidC. Despite the importance of YidC, the precise function and mechanism of this protein are difficult to define. In our lab we are using Fluorescence Resonance Energy Transfer (FRET) to monitor structural changes of an inner membrane protein during synthesis on the ribosome, targeting to the YidC pathway and integration into the membrane. This technique enables us to monitor the compaction of α-helices and the formation of tertiary structure, in order to elucidate the timing of folding events that occue between the ribosome exit tunnel and the adoption of the final functional conformation in the membrane. The findings are supported by in vitro insertion assays and crosslinking to the signal recognition (SRP), which provide further details of the role of SRP in YidC targeting.
Publications
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Peterson, J.H., Woolhead, C.A. and Bernstein, H.D. (2010) The conformation of a nascent polypeptide inside the ribosome tunnel affects protein targeting and protein folding. Molecular Microbiology, 78(1), pp. 203-217.
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Cabrita, L. D. et al. (2016) A structural ensemble of a ribosome–nascent chain complex during cotranslational protein folding. Nature Structural and Molecular Biology, 23(4), pp. 278-285.
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Robinson, P. J., Pringle, M. A., Woolhead, C. A. and Bulleid, N. J. (2017) Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation. Journal of Biological Chemistry, 292(17), pp. 6978-6986.
