Understanding the yeast host cell response to recombinant membrane protein production

Zharain Bawa, Charlotte E. Bland, Nicklas Bonander, Nagamani Bora, Stephanie P. Cartwright, Michelle Clare, Matthew T. Conner, Richard A.J. Darby, Marvin V Dilworth, William J. Holmes, Mohammed Jamshad, Sarah J. Routledge, Stephane R. Gross, Roslyn M. Bill

Research output: Contribution to journalArticlepeer-review


Membrane proteins are drug targets for a wide range of diseases. Having access to appropriate samples for further research underpins the pharmaceutical industry's strategy for developing new drugs. This is typically achieved by synthesizing a protein of interest in host cells that can be cultured on a large scale, allowing the isolation of the pure protein in quantities much higher than those found in the protein's native source. Yeast is a popular host as it is a eukaryote with similar synthetic machinery to that of the native human source cells of many proteins of interest, while also being quick, easy and cheap to grow and process. Even in these cells, the production of human membrane proteins can be plagued by low functional yields; we wish to understand why. We have identified molecular mechanisms and culture parameters underpinning high yields and have consolidated our findings to engineer improved yeast host strains. By relieving the bottlenecks to recombinant membrane protein production in yeast, we aim to contribute to the drug discovery pipeline, while providing insight into translational processes.
Original languageEnglish
Pages (from-to)719-723
Number of pages5
JournalBiochemical Society Transactions
Issue number3
Publication statusPublished - Jun 2011

Bibliographical note

This research was originally published in Biochemical Society transactions. Bawa, Z, Bland, CE, Bonander, N, Bora, N, Cartwright, SP, Clare, M, Conner, MT, Darby, RA, Dilworth, MV, Holmes, WJ, Jamshad, M, Routledge, SJ, Gross, SR & Bill, RM 2011, 'Understanding the yeast host cell response to recombinant membrane protein production', Biochemical Society transactions, vol 39, no. 3, pp. 719-723. © the Biochemical Society.


  • bioengineering
  • humans
  • membrane proteins
  • recombinant proteins
  • saccharomyces cerevisiae
  • yeasts


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