Cloning and expression of the exo-beta-D-1,3-glucanase gene (exgS) from Aspergillus saitoi.
A gene of exo-1,3-beta-D-glucanase (exgS) was cloned from a koji mold, Aspergillus saitoi, genomic DNA using PCR. The exgS has an ORF comprising 2832 bp, which contains one intron of 45 bp, and encodes 945 amino acids. The deduced amino acid sequences showed that the ExgS has a non-homologous linker region consisting of 180 amino acids, which encompassed highly conserved regions observed in Exg homologues from filamentous fungi. A recombinant protein (ExgS) has been recovered from the cultural filtrate of an Aspergillus oryzae strain that carried an expression vector containing full length of the exgS. The N-terminal amino acid sequences of the recombinant exo-1,3-beta-D-glucanase (ExgS) were identical to that of native ExgS from A. saitoi.
Oda
Ken
K
Laboratory of Enzymology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan. odaken@biochem.tohoku.ac.jp
Kasahara
Shin
S
Yamagata
Youhei
Y
Abe
Keietsu
K
Nakajima
Tasuku
T
D000595:Amino Acid Sequence; D001230:Aspergillus / Q000201:enzymology* / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D015971:Gene Expression Regulation, Enzymologic / Q000235:genetics*; D015966:Gene Expression Regulation, Fungal / Q000235:genetics*; D005800:Genes, Fungal / Q000235:genetics; D006026:Glycoside Hydrolases / Q000235:genetics*; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction
D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; C021780:exo-1,3-alpha-glucanase