Dynamic Live Cell Imaging

Dynamic Live Cell Imaging at Sub-zero Temperatures

Start date
2 January, 2025
End date
2 January, 2027

Dynamic live cell imaging at sub-zero temperatures

How do Antarctic marine organisms, such as fish, manage to thrive at temperatures below 0°C? How do their cells and in particular, their proteins function in extreme cold?

Why is this important?

Proteins are key building blocks for life with functions that are uniquely dependent on their 3-Dimensional folded state. Whilst much is known about the constraints on how proteins operate at high temperatures, little knowledge exists about how biology operates at all scales of life in sub-zero conditions where proteins are less stable and oxidative damage is high. Almost 90% of habitable environments on Earth are permanently below 5 degrees (i.e. deep sea and polar regions). This means we do not understand how a large proportion of global biodiversity functions at such low temperatures. It is particularly critical to address this knowledge gap, given the current climate crisis and impeding large-scale loss of the planet’s colder regions and their endemic biodiversity.

 

Contact for further information: Melody Clark mscl@bas.ac.uk

 

This exciting new collaboration between BAS and the Department of Chemical Engineering and Biotechnology, University of Cambridge aims to understand how proteins operate in situ in living cells at temperatures of 0°C and below, using fish cell cultures from the Antarctic plunderfish Harpagifer antarcticus.

The spiny plunderfish ( Harpagifer antarcticus ) lying on rocks covered with pink encrusting algae ( Lithothamnion ) showing its excellent camouflage capabilities.
The spiny plunderfish (Harpagifer antarcticus) lying on rocks covered with pink encrusting algae (Lithothamnion) showing its excellent camouflage capabilities.

We will take some of the most advanced imaging tools available and, for the first time, adapt them to work with Antarctic species to study their cellular biology, in particular the folding behaviours of proteins, in conditions that mimic their extreme natural environments.