Molecular cloning and characterization of two novel cellulase genes from the mollusc Ampullaria crossean.
Cellulase genes have been reported not only from fungi, bacteria and plant, but also from some invertebrate animals. Here, two cellulase (endo-beta-1,4-glucanase, EC 3.2.1.4) genes, eg27I and eg27II, were cloned from the freshwater snail Ampullaria crossean cDNA using degenerate primers. The nucleotide sequences of the two genes shared 94.5% identity. The open reading frames of both genes consisted of 588 bp, encoding 195 amino acids. Both EG27I and EG27II belong to the glycoside hydrolase family 45, and each lacks a carbohydrate-binding module. The presence of introns demonstrated a eukaryotic origin of the EG27 gene, and, in addition, successful cloning of EG27 cDNA supported endogenous production of EG27 cellulase by Ampullaria crossean. Investigation of the EG27 cDNA from A. crossean will provide further information on GHF45 cellulases.
Guo
Rui
R
State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China. pretty_rui@msn.com
Ding
Ming
M
Zhang
Si-Liang
SL
Xu
Gen-Jun
GJ
Zhao
Fu-Kun
FK
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002480:Cellulase / Q000235:genetics*; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D019143:Evolution, Molecular; D015971:Gene Expression Regulation, Enzymologic; D007438:Introns / Q000235:genetics; D008969:Molecular Sequence Data; D008974:Mollusca / Q000201:enzymology* / Q000235:genetics*; D010802:Phylogeny
D018076:DNA, Complementary; D002480:Cellulase