Cloning and characterization of farnesyl pyphosphate synthase gene from the ABA-producing fungi Botrytis cinerea.
Farnesyl pyphosphate synthase (FPPS) catalyzes the systhesis of farnesyl pyphosphate and appears to be a promising regulation site of Abscisic acid (ABA) biosynthesis pathway in fungi. Here we reported the isolation and characterization of Botrytis cinerea (FPPS) gene. The cloned FPPS gene carries an open reading frame of 1044-bp encoding a deduced protein of 347 amino acids with a molecular weight of 39.83 kDa, and the coding region is interrupted with a 63-bp intron. Comparison analysis showed that the deduced amino acids sequence share high similarity with other known FPPS gene. Southern blot revealed a single copy of FPPS gene in the genomic DNA. The result of transcription analysis indicated that the cloned FPPS gene expressed constitutively and was not induced in ABA accumulation phase.
Deng
Hong-Yuan
HY
Chengdu Institute of Biology, The Chinese Academy of Sciences, Chengdu, People's Republic of China.
Ma
Xin-Rong
XR
Li
Zhi-Dong
ZD
Tan
Hong
H
D000040:Abscisic Acid / Q000096:biosynthesis*; D000595:Amino Acid Sequence; D001483:Base Sequence; D020171:Botrytis / Q000201:enzymology* / Q000235:genetics*; D003001:Cloning, Molecular; D015966:Gene Expression Regulation, Fungal; D051228:Geranyltranstransferase / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data
D000040:Abscisic Acid; D051228:Geranyltranstransferase