The first crystal structures of recombinant
mammalian membrane proteins were solved in 2005 using protein that had
been produced in yeast cells. One of these, the rabbit Ca2+-ATPase SERCA1a, was synthesized in Saccharomyces cerevisiae.
All host systems have their specific advantages and disadvantages, but
yeast has remained a consistently popular choice in the eukaryotic
membrane protein field because it is quick, easy and cheap to culture,
whilst being able to post-translationally process eukaryotic membrane
proteins. Very recent structures of recombinant membrane proteins
produced in S. cerevisiae include those of the Arabidopsis thaliana
NRT1.1 nitrate transporter and the fungal plant pathogen lipid
scramblase, TMEM16. This chapter provides an overview of the
methodological approaches underpinning these successes.