Abstract：Plant cellulose synthase is one of important glycosyltransferases, which catalytic synthesis a paracrystalline form of H-bonded-β-1, 4-Glc chains. In this study, a unigene that was highly homologous to the Zea Mays cellulose synthase 3 (Ces3) sequence was isolated from the sugarcane (Saccharum officinarum) full-length cDNA library in response to water stress. The full-length sequence was to obtain by reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends (RACE), contained most 5'-end excluding 80 bp and the whole 3'-end with poly (A), named as ScCes3 (GenBank No. MG324347). ScCes3 had a full-length cDNA sequence of 3 625 bp and contained a contained open reading frame (3 225 bp), encoding 1 074 amino acids. Bioinformatics prediction indicated that ScCes3 was stable amphoterin protein located in cell plasmalemma, and had no signal peptide but with random coil according to its secondary structure. The ScCes3 protein contained the conservative domains of plant cellulose synthase proteins. qRT-PCR results indicated the expression of ScCes3 could be found in leaf, leaf sheath and stem. The high expression level in stem, especially with the highest expression level in No.5 stem, and lowly in leaf. This study has established a foundation for future research on gene expression and funtion analysis.
