MOLECULAR CHARACTERIZATION OF A CDNA-ENCODING CHLOROPLASTIC FRUCTOSE-1,6-BISPHOSPHATASE FROM SOYBEAN (GLYCINE-MAX L.)

A full-length cDNA of soybean chloroplastic fructose-1,6-bisphosphatas e was cloned and sequenced. The cDNA contained 1321 bp with 5' (26 bp) and 3' (88 bp) untranslated regions, The open reading frame of the cD NA contained 1206 bp corresponding to a polypeptide of 402 amino acids with 50 amino acid residues of a transit peptide at N-terminus that i s necessary for transport into the chloroplast. A unique site relevant to the action of thioredoxin f was conserved at 221 amino acid residu e. Northern blot analysis indicated that the expression of the enzyme was regulated by light illumination.