Open AccessGenome structure and nucleotide sequence of a lipolytic enzyme gene of Aspergillus oryzae
Author(s) -
Ohnishi Kunio,
Toida Jinichi,
Nakazawa Hidekazu,
Sekiguchi Junichi
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07408.x
Subject(s) - aspergillus oryzae , gene , nucleic acid sequence , biology , genetics , enzyme , aspergillus , nucleotide , genome , sequence (biology) , biochemistry
Aspergillus oryzae , which is widely used for Japanese traditional fermentation, produced at least two lipolytic enzymes (L1 and L2). Southern hybridization analysis of restriction enzyme‐digested genomic DNA fragments of Aspergillus oryzae with 23‐mer oligonucleotides synthesized according to the amino acid sequence of the enzyme L1 as probes suggested that there is single copy of the L1 gene in the genome. DNA fragments containing the L1 gene were cloned in Escherichia coli . Nucleotide sequencing of the DNA fragments revealed an open reading frame consisting of 213 amino acid residues. It had three putative introns whose sizes were 52 bp, 48 bp and 53 bp, respectively. Putative CAAT and TATA boxes were found at positions −147 and −100 from A (+1) of the translational initiation codon, and a polyadenylation site at 158 bp downstream of the stop codon. The deduced amino acid sequence of the L1 gene was highly similar to those of cutinases from phytopathogenic fungi. Thus, it is interesting to note that the non‐phytopathogenic fungus, A. oryzae , produces cutinase, which seems to play an important role in flavor formation.