Cloning and characterization of the gene encoding endo-beta-1,3-glucanase from Arthrobacter sp. NHB-10

• Published in: Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2007-06, Vol.71 (6), p.1568-1571
• Main Authors: Okazaki, K.(Kagawa Univ., Miki (Japan). Faculty of Agriculture), Nishimura, N, Matsuoka, F, Hayakawa, S
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; AMINO ACID SEQUENCES; ARTHROBACTER; Arthrobacter - enzymology; Arthrobacter - genetics; Arthrobacter sp; Base Sequence; BETA GLUCANASA; BETA GLUCANASE; Biological and medical sciences; Catalytic Domain; CLONACION MOLECULAR; CLONAGE MOLECULAIRE; Cloning, Molecular; Conserved Sequence; endo-β-1,3-glucanase; Fundamental and applied biological sciences. Psychology; GENE; gene cloning; Gene Components; GENES; GLICOSIDOS; Glucan Endo-1,3-beta-D-Glucosidase - genetics; GLYCOSIDE; GLYCOSIDES; MOLECULAR CLONING; Molecular Sequence Data; PEPTIDE; PEPTIDES; PEPTIDOS; SECUENCIAS DE AMINOACIDOS; Sequence Alignment; SEQUENCE D'ACIDES AMINES; Sequence Homology, Nucleic Acid; STREPTOMYCES; Streptomyces coelicolor
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.70030

The gluA gene, encoding an endo-beta-1,3-glucanase from Arthrobacter sp.(strain NHB-10), was cloned and analyzed. The deduced endo-beta-1,3-glucanase amino acid sequence was 750 amino acids long and contained a 42 amino acid signal peptide with a mature protein of 708 amino acids. There was no similarity to known endo-beta-1,3-glucanases, but GluA was partially similar to two fungal exo-beta-1,3-glucanases in glycoside hydrolase(GH) family 55. Of five possible residues for catalysis and two motifs in two beta-helix heads of GH family 55, three residues and one motif were conserved in GluA, suggesting that GluA is the first bacterial endo-beta-1,3-glucanase in GH family 55. Significant similarity was also found to two proteins of unknown function from Streptomyces coelicolor A3(2) and S. avermitilis.