Isolation, sequence and bacterial expression of a cDNA for chalcone synthase from the cultured cells of Pueraria lobata.
cDNA clones for chalcone synthase (CHS) of Pueraria lobata cultured cells were isolated by screening the cDNA library using CHS cDNA of Phaseolus vulgaris as a probe. Analysis of nucleotide sequences of the cloned cDNA revealed a 1170-bp open reading frame that encoded a 390-amino acid polypeptide with an Mr of 43,000. The full-length cDNA was cloned into the expression vector pT7-7. CHS activity was found in the crude extracts of transformed E. coli after induction and two protein bands of ca. 43 and 34 kd were hybridized with anti-persley CHS antiserum.
Nakajima
O
O
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Akiyama
T
T
Hakamatsuka
T
T
Shibuya
M
M
Noguchi
H
H
Ebizuka
Y
Y
Sankawa
U
U
D000217:Acyltransferases / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics* / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology*
D004247:DNA; D000217:Acyltransferases; C020141:flavanone synthetase