Molecular analysis of a novel protein kinase in maturing rice seed.

Protein kinases play important roles in controlling biological functions. We employed PCR-based cloning technique to isolate a protein kinase gene from rice endosperm and obtained a novel protein kinase (REK) cDNA clone from a cDNA library constructed from maturing rice seed. The deduced amino acid sequence from the cDNA exhibited a high similarity to the wheat abscisic acid inducible protein kinase (PKABA1), including 11 conserved regions of the catalytic domain. REK belongs to the SNF1-related family that possesses abundant acidic amino acid resides in the C-terminal region. RT-PCR analysis showed that the REK gene is expressed in leaf and maturing seed, but not in stem and root. Bacterial recombinant REK showed autophosphorylation activity depending upon Ca2+. In addition, we isolated a REK genomic clone and determined its gene structure.