Michigami Y, Watabe S, Abe K, Obata H, Arai S
Department of Agricultural Chemistry, University of Tokyo, Japan.
Biosci Biotechnol Biochem. 1994 Apr;58(4):762-4. doi: 10.1271/bbb.58.762.
An ice nucleation activity gene, named inaU, of the bacterium Erwinia uredovora KUIN-3 has been sequenced. This gene encodes a protein of 1034 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 the inaU protein is similar to those of the inaA, inaW, and inaZ gene products of Erwinia ananas, Pseudomonas fluorescens, and Pseudomonas syringae, respectively, but is smaller than any of these products in terms of the size of the R-domain.
对杏黄欧文氏菌KUIN - 3的一个名为inaU的冰核活性基因进行了测序。该基因编码一个含有1034个氨基酸残基的蛋白质，其表达产物inaU蛋白有一个由52个紧密相关的16氨基酸基序重复序列（R结构域）组成的832个氨基酸残基片段，两侧分别为N端和C端序列（分别为N结构域和C结构域）。inaU蛋白的一级结构分别与菠萝欧文氏菌的inaA、荧光假单胞菌的inaW和丁香假单胞菌的inaZ基因产物相似，但就R结构域的大小而言，比这些产物中的任何一个都小。
