Ice nucleation proteins self-assemble into large fibres to trigger freezing at near 0 °C.

ABSTRACT: In nature, frost can form at a few degrees below 0 °C. However, this process requires the assembly of tens of thousands of ice-like water molecules that align together to initiate freezing at these relatively high temperatures. Water ordering on this scale is mediated by the ice nucleation proteins of common environmental bacteria like Pseudomonas syringae and P. borealis. However, individually, these 100-kDa proteins are too small to organize enough water molecules for frost formation, and it is not known how giant, megadalton-sized multimers, which are crucial for ice nucleation at high sub-zero temperatures, form. The ability of multimers to self-assemble was suggested when the transfer of an ice nucleation protein gene into Escherichia coli led to efficient ice nuc

SUBMITTER: Hansen T 

PROVIDER: S-EPMC10418271 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature