Cloning of a novel crystal protein gene cry1K from Bacillus thuringiensis subsp. morrisoni

A novel crystal protein gene cry1K has been cloned and sequenced from a Bacillus thuringiensis subsp. morrisoni BF190 isolated from phylloplane. The upstream promoter region of cry1K was almost identical with that of cry1B. The deduced amino acid sequence of Cry1K contains 1215 amino acid residues with an estimated molecular mass of 137 kDa. Comparison of the amino acid sequence of the Cry1K with that of Cry proteins revealed that Cry1K is most closely related to Cry1B and Cry1I. Cry1K has a high degree of identity with Cry1B in the region between initiator codon and conserved sequence block 1, and with Cry1F in the region between conserved block 3 and 5. Protein inclusion purified from a recombinant strain of B. thuringiensis expressing the cry1K gene was found to have a different insect-host specificity from Cry1B, Cry1I and Cry1F, Cry1K was found to be selectively toxic to Artogeia rapae and not active to Plutella xylostella.