Cloning of cellulose synthase genes from Acetobacter xylinum JCM 7664: implication of a novel set of cellulose synthase genes

• Published in: DNA research 1999, Vol.6 (2), p.109-115
• Main Authors: Umeda, Y, Hirano, A, Ishibashi, M, Akiyama, H, Onizuka, T, Ikeuchi, M, Inoue, Y
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Arabidopsis Proteins; Base Sequence; Cloning, Molecular; DNA Primers; Genes, Bacterial; Gluconacetobacter xylinus - enzymology; Gluconacetobacter xylinus - genetics; Glucosyltransferases - genetics; Molecular Sequence Data; Multigene Family; Open Reading Frames; Restriction Mapping; Sequence Homology, Amino Acid
• ISSN: 1340-2838
• DOI: 10.1093/dnares/6.2.109

Three sets of cellulose synthase genes were cloned from a cellulose-producing bacterium Acetobacter xylinum JCM 7664. One set of genes (bcsAI/bcsBI/bcsCI/bcsDI) were highly conserved with the well-established type I genes in other strains of A. xylinum, while the other two (bcsABII-A, bcsABII-B) were homologous to the known type II (acsAII). Unexpectedly, they were immediately followed by a gene cluster of bcsX/bcsY/bcsCII/ORF569, likely forming an operon. Western blotting demonstrated that the BcsY protein accumulated in cells. Since BcsY showed striking similarities to a number of membrane-bound transacylases, it was hypothesized that the type II cellulose synthase produces acylated cellulose, which might be anchored on the cytoplasmic membrane. An insertion sequence of IS1380-type was found just upstream of the one type II gene (bcsABII-B), suggestive of nonfunctioning.