Water-organizing motif continuity is critical for potent ice nucleation protein activity

Jordan Forbes, Akalabya Bissoyi, Lukas Eickhoff, Naama Reicher, Thomas Hansen, Christopher G. Bon, Virginia K. Walker, Thomas Koop, Yinon Rudich, Ido Braslavsky and Peter L. Davies ()
Additional contact information
Jordan Forbes: Queen’s University
Akalabya Bissoyi: The Hebrew University of Jerusalem
Lukas Eickhoff: Bielefeld University, Faculty of Chemistry
Naama Reicher: The Weizmann Institute of Science
Thomas Hansen: Queen’s University
Christopher G. Bon: Queen’s University
Virginia K. Walker: Queen’s University
Thomas Koop: Bielefeld University, Faculty of Chemistry
Yinon Rudich: The Weizmann Institute of Science
Ido Braslavsky: The Hebrew University of Jerusalem
Peter L. Davies: Queen’s University

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: Abstract Bacterial ice nucleation proteins (INPs) can cause frost damage to plants by nucleating ice formation at high sub-zero temperatures. Modeling of Pseudomonas borealis INP by AlphaFold suggests that the central domain of 65 tandem sixteen-residue repeats forms a beta-solenoid with arrays of outward-pointing threonines and tyrosines, which may organize water molecules into an ice-like pattern. Here we report that mutating some of these residues in a central segment of P. borealis INP, expressed in Escherichia coli, decreases ice nucleation activity more than the section’s deletion. Insertion of a bulky domain has the same effect, indicating that the continuity of the water-organizing repeats is critical for optimal activity. The ~10 C-terminal coils differ from the other 55 coils in being more basic and lacking water-organizing motifs; deletion of this region eliminates INP activity. We show through sequence modifications how arrays of conserved motifs form the large ice-nucleating surface required for potency.

Date: 2022
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DOI: 10.1038/s41467-022-32469-9

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