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Showing results 1 to 4 of 4
  • OER000000796.pdf.jpg
  • Journal article

  • Distinct metabolic states of a cell guide alternate fates of mutational buffering through altered proteostasis

    • Authors : Verma, Kanika; Saxena, Kanika; Donaka, Rajashekar (2020)

  • Changes in metabolism can alter the cellular milieu; can this also change intracellular proteostasis? Since proteostasis can modulate mutational buffering, if change in metabolism has the ability to change proteostasis, arguably, it should also alter mutational buffering. Building on this, we find that altered cellular metabolic states in E. coli buffer distinct mutations. Buffered-mutants had folding problems in vivo and were differently chaperoned in different m...
  • OER000002770.pdf.jpg
  • Journal article

  • Engineering a more specific E. coli glyoxylate/hydroxypyruvate reductase for coupled steady state kinetics assays

    • Authors : Vuksanovic, Nemanja (2023)

  • The E. coli glyoxylate reductase/hydroxypyruvate reductase A (EcGhrA) was investigated as a coupling enzyme to monitor the transamination of 2-ketoarginine and glycine by the L-enduracididine biosynthetic enzyme MppQ. Surprisingly, 2-ketoarginine proved to be an efficient substrate for EcGhrA. Since the promiscuity of EcGhrA prevented its use as a coupling enzyme to monitor the aminotransferase activity of MppQ, we set about engineering a more specific variant.&#x...
  • OER000003007.pdf.jpg
  • Journal article

  • Identification and assessment of cardiolipin interactions with E. coli inner membrane proteins

    • Authors : Corey, Robin A. (2021)

  • Integral membrane proteins are localised and/or regulated by lipids present in the surrounding bilayer. Whilst bacteria such as E. coli have relatively simple membranes when compared to eukaryotic cells, there is ample evidence that many bacterial proteins bind to specific lipids, especially the anionic lipid cardiolipin. Here, we apply molecular dynamics simulations to assess lipid binding to 42 different E. coli inner membrane proteins. O...
  • OER000002711.pdf.jpg
  • Journal article

  • Zur and Zinc Increase Expression of E. coli Ribosomal Protein L31 Through RNA-Mediated Repression of the Repressor L31p

    • Authors : Rasmussen, Rebecca A. (2023)

  • Bacteria can adapt in response to numerous stress conditions. One such stress condition is zinc depletion. The zinc-sensing transcription factor Zur regulates the way enteric bacteria respond to severe changes in zinc availability. Under zinc sufficient conditions, Zn-loaded Zur (Zn2-Zur) is well-known to repress transcription of genes encoding zinc uptake transporters and paralogues of a few ribosomal subunits. Here, we report the discovery and mechanistic basis&...