Heterologous Expression and Secretion of Cell Cycle Proteins Using the Yeast Picchia pastoris

Abstract

Bacterial and baculoviral expressions are the two current systems of choice for protein expression (see Hannon and Connel-Crowley and Harper, this Vol.). However, these methods cannot combine the same advantages (see discussion in Hannon, this Vol.) Here, the use of an emerging protein expression technology which conciliates the major benefits of bacterial and baculoviral protein expression is described. Proteins can be produced in high amounts either intra- or extracellularly, allowing an extremely effective protein purification. Moreover, as it uses an eukaryotic host protein processing, folding and post-translational modifications can occur and, as the host is a yeast cell, maintenance and growth even in high volume (fermentation) are fast, easy and economical.