Y. Michigami et al., CLONING AND SEQUENCING OF AN ICE NUCLEATION ACTIVE GENE OF ERWINIA-UREDOVORA, Bioscience, biotechnology, and biochemistry, 58(4), 1994, pp. 762-764
An ice nucleation activity gene, named inaU, of the bacterium Erwinia
uredovora KUIN-3 has been sequenced. This gene encodes a protein of 10
34 amino acid residues, and its expression product, inaU protein, has
an 832-amino acid residue segment consisting of 52 repeats of closely
related 16-amino acid motifs (R-domain), flanked by N- and C-terminal
sequences (N- and C-domains, respectively). The primary structure of t
he inaU protein is similar to those of the inaA, inaW, and inaZ gene p
roducts of Erwinia ananas, Pseudomonas fluorescens, and Pseudomonas sy
ringae, respectively, but is smaller than any of these products in ter
ms of the size of the R-domain.