Molecular characterization of the gene encoding rice allene oxide synthase and its expression.
The gene encoding rice allene oxide synthase, OsAOS, was intronless and had nucleotide sequences with the high GC content of 67%. Deduced amino acid sequences had very high similarity with other AOS proteins, in particular 74% similarity to barley, characterized by the conserved motifs of P450 cytochrome of the CYP74A family. Purified recombinant rice AOS protein expressed in Escherichia coli converted 13-hydroperoxylinolenic acid to allene oxide. Several restriction enzyme digestions and Southern analysis showed that OsAOS was likely to have two copies in its genome. The basal level of OsAOS expression was detected in various tissues and the transcription level was increased by jasmonate treatment.
Ha
Suk-Bong
SB
Department of Genetic Engineering, Biotechnology Research Institute, Chonnam National University, Gwangju 500-757, Korea.
Lee
Bong-Choon
BC
Lee
Da-Eun
DE
Kuk
Yong In
YI
Lee
A-Young
AY
Han
Oksoo
O
Back
Kyoungwhan
K
D000595:Amino Acid Sequence; D003517:Cyclopentanes / Q000494:pharmacology; D020869:Gene Expression Profiling; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects; D019746:Intramolecular Oxidoreductases / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D012275:Oryza / Q000201:enzymology* / Q000235:genetics*; D054883:Oxylipins; D016415:Sequence Alignment
D003517:Cyclopentanes; D054883:Oxylipins; C011006:jasmonic acid; D019746:Intramolecular Oxidoreductases; C021377:hydroperoxide isomerase