A new full-length acyltransferase cDNA was obtained from Taxus chinensis by homologybased cloning strategy. The cDNA has an open-reading frame of 1,275 nucleotides, which encodes 425 amino acids with a calculated mole cular weight of 47,241 Da and an estimated pI value of 5.93. The deduced amino acid sequence resembles the sequences of other cloned acyltransferases (56-61% identity; 71-75% imilarity) involved directly in taxol biosynthetic pathways. This cDNA was expressed in Escherichia coli using the expression vector pET-32a(+). The expression band corresponds to the calculated mass plus the N-terminal fusion protein derived from the vector.