Structural and functional investigations of bdellovibrio bacteriovorus lifecycle proteins


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Harding, Christopher John (2019). Structural and functional investigations of bdellovibrio bacteriovorus lifecycle proteins. University of Birmingham. Ph.D.

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This thesis documents the findings undertaken on a diverse set of proteins that operate at distinct stages of the predatory lifecycle of Bdellovibrio bacteriovorus. In general, this work explores three major predatory lifecycle events: growth & metabolism, development & signalling and finally bdelloplast lysis & exit. In particular this thesis characterises four individual proteins (Bd2924, Bd1833, Bd0967 and Bd0314) that perform very different roles.

In this study the three dimensional structure of Bd2924 (a putative acyl-CoA dehydrogenase) was determined, demonstrating an adaptation of the common acyl-CoA dehydrogenase fold, suggesting an important role beyond fatty acid β-oxidation. This work also presents the first structure of a multi-modular malic enzyme (Bd1833) and through extensive mutational and biochemical investigations, the mechanism behind allosteric regulation by acetyl-CoA was unpicked. In addition the structure of Bd0967 (a C-terminal processing protease) was solved, revealing a divergent fold that forms a large self-compartmentalised cavity. Furthermore, Bd0967 was determined to be involved in a developmental pathway that is interconnected with flagellin assembly. Finally, this study reveals how Bdellovibrio uses an adapted lysozyme (Bd0314), remodeled into a variant that now only accepts deacetylated cell wall sugars to lyse the bdelloplast at the end of the predatory lifecycle.

Type of Work: Thesis (Doctorates > Ph.D.)
Award Type: Doctorates > Ph.D.
Licence: All rights reserved
College/Faculty: Colleges (2008 onwards) > College of Life & Environmental Sciences
School or Department: School of Biosciences
Funders: None/not applicable
Subjects: Q Science > QR Microbiology


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