Membrane protein production in the Yeast, S. cerevisiae

Stephanie P. Cartwright, Lina Mikaliunaite, Roslyn M. Bill

Research output: Chapter in Book/Published conference outputChapter (peer-reviewed)peer-review


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.

Original languageEnglish
Title of host publicationHeterologous expression of membrane proteins
EditorsIsabelle Mus-Veteau
Place of PublicationNew York (US)
Number of pages13
ISBN (Electronic)978-1-4939-3637-3
ISBN (Print)978-1-4939-3635-9
Publication statusPublished - 3 Aug 2016

Publication series

NameMethods in Molecular Biology
ISSN (Print)064-3745


  • membrane protein
  • recombinant
  • S. cerevisiae
  • P GAL promoter


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