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-bisphosphatase 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 cDNA contained 1206 bp corresponding to a polypeptide of 402 amino acids with 50 amino acid residues of a transit peptide at N-terminus that is necessary for transport into the chloroplast. A unique site relevant to the action of thioredoxin f was conserved at 221 amino acid residue. Northern blot analysis indicated that the expression of the enzyme was regulated by light illumination.
Jeon
Y H
YH
Department and Institute of Genetic Engineering, Kyung Hee University, Suwon, Korea.
Bhoo
S H
SH
Hahn
T R
TR
D000595:Amino Acid Sequence; D001483:Base Sequence; D002736:Chloroplasts / Q000201:enzymology* / Q000235:genetics*; D018742:DNA, Chloroplast / Q000737:chemistry / Q000302:isolation & purification; D018076:DNA, Complementary / Q000737:chemistry*; D004789:Enzyme Activation / Q000528:radiation effects; D006597:Fructose-Bisphosphatase / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D008027:Light; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D013025:Glycine max / Q000201:enzymology* / Q000235:genetics*
D018742:DNA, Chloroplast; D018076:DNA, Complementary; D006597:Fructose-Bisphosphatase