Publications by authors named "Lorna E Lancaster"

Article Synopsis
  • The study investigates the effects of intrinsic disorder in proteins, focusing on the colicin E3 rRNase domain and its interaction with the Im3 protein.
  • An alanine mutation turns the colicin E3 rRNase into an intrinsically disordered protein (IDP), which still binds to Im3 but with significantly weaker affinity.
  • The research highlights that while intrinsic disorder can be beneficial, it results in a notable reduction in binding strength and kinetic efficiency, demonstrating a trade-off between flexibility and stability in protein interactions.
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Strains of Clostridium difficile produce toxins A and B that can cause diarrhoea and pseudomembranous colitis. Currently, there is no preventative therapy for this infection but antibodies to the toxins provide protection, therefore a toxoid-based vaccine is needed. To evaluate thermal stability, a lyophilized and liquid formulation of toxoids A and B were stored at a range of temperatures for 5 weeks.

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The cytotoxin colicin E3 targets the 30S subunit of bacterial ribosomes and specifically cleaves 16S rRNA at the decoding centre, thereby inhibiting translation. Although the cleavage site is well known, it is not clear which step of translation is inhibited. We studied the effects of colicin E3 cleavage on ribosome functions by analysing individual steps of protein synthesis.

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Colicins are a family of antibacterial cytotoxins produced by Escherichia coli and released into the environment to reduce competition from other bacterial strains. Colicins kill the target cell by a variety of effects that include depolarisation of the cytoplasmic membrane, a non-specific DNase activity, a highly specific RNase activity or by inhibition of murein synthesis. This review summarises some important findings that implicate colicins as potential anti-tumor agents.

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