Cloning and structural analysis of bglM gene coding for the fungal cell wall-lytic beta-1,3-glucan-hydrolase BglM of Bacillus circulans IAM1165.
Bacillus circulans IAM1165 produces isoforms of beta-1,3-glucan-hydrolases. Of these enzymes, the 42-kDa enzyme BgIM degrades Aspergillus oryzae cell walls the most actively. A gene coding for a BgIM precursor consisting of 411 amino acid residues was cloned. The 27 N-terminal amino acid sequence of the precursor is a signal peptide. The 141 C-terminal amino acid sequence showed a motif of carbohydrate-binding module family 13. This domain bound to pachyman, lichenan, and A. oryzae cell walls. The central domain showed a bacterial beta-1,3-glucan-hydrolase motif belonging to glycosyl hydrolase family 16. By removal of the C-terminal domain in the IAM1165 culture, mature BglM was processed to several 27-kDa fragments that hydrolyze a soluble beta-1,3-glucan.
Asano
Takeshi
T
Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Taki
Jiro
J
Yamamoto
Mami
M
Aono
Rikizo
R
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology* / Q000235:genetics*; D001483:Base Sequence; D001665:Binding Sites; D002473:Cell Wall / Q000378:metabolism*; D002876:Chromosomes, Bacterial / Q000235:genetics; D003001:Cloning, Molecular; D005658:Fungi / Q000166:cytology*; D005798:Genes, Bacterial / Q000235:genetics*; D005959:Glucosidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D011134:Polysaccharides / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid
D011134:Polysaccharides; D005959:Glucosidases