A new ice nucleation gene from Pseudomonas syringae was isolated and o
verexpressed as a fully active protein in Escherichia coli in order to
gain experimental data about the structure of ice nucleation proteins
, No evidence of a signal sequence or secondary glycosylation was foun
d, Differences in the extent of aggregation were shown to modulate the
ice nucleation activity. The circular dichroism spectrum of the purif
ied protein indicated the presence of beta-sheet structure, This findi
ng supports a recently proposed hypothetical model for the structure o
f ice nucleation proteins, which provides a plausible explanation for
their aggregation tendency. (C) 1997 Federation of European Biochemica
l Societies.