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Head of Institute: Prof. Ido Braslavsky

Administrative manager: Rakefet Kalev

Office Address:
Institute of Biochemistry, Food Science and Nutrition,
Robert H. Smith Faculty of Agriculture, Food and Environment,
The Hebrew University of Jerusalem, 
Herzl 229, Rehovot 7610001, ISRAEL

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

Citation:

Forbes, J. ; Bissoyi, A. ; Eickhoff, L. ; Reicher, N. ; Hansen, T. ; Bon, C. G. ; Walker, V. K. ; Koop, T. ; Rudich, Y. ; Braslavsky, I. ; et al. Water-organizing motif continuity is critical for potent ice nucleation protein activity. 2022, 13, 5019.

Date Published:

2022

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.

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