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Planta, Vol. 216 (2003) pp. 597 - 603
© 2002 Springer-Verlag All rights reserved.

Expression and localization of human lysozyme in the endosperm of transgenic rice.
Daichang Yang, Fengli Guo, Bo Liu, Ning Huang, Simon C. Watkins

In order to understand the characteristics of recombinant protein expression and sublocalization in rice (Oryza sativa L.) endosperm, we examined the expression level of human lysozyme protein and its sub-cellular location in transgenic rice seeds driven by rice glutelin and globulin promoters and signal peptides. A time course of human lysozyme expression during endosperm development was analyzed. The results showed that the expression profile of recombinant protein accumulation in endosperm paralleled that of the two storage proteins. Immunofluorescense microscopy revealed that human lysozyme and storage proteins colocalized to type-II protein bodies. Both promoter-signal peptide pairings targeted recombinant protein to the protein bodies. In addition, a transgenic line with a higher lysozyme expression level exhibited morphologically different protein bodies with an unbalanced composition of lysozyme and native storage proteins. The high-level expression of recombinant protein distorted the trafficking and sorting of native storage proteins in rice endosperm and affected the expression of native storage protein. © 2002 Springer-Verlag All rights reserved.