Chapter title |
Heterologous Expression of Membrane Proteins
|
---|---|
Chapter number | 2 |
Book title |
Heterologous Expression of Membrane Proteins
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3637-3_2 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3635-9, 978-1-4939-3637-3
|
Authors |
Cartwright, Stephanie P, Mikaliunaite, Lina, Bill, Roslyn M, Stephanie P. Cartwright, Lina Mikaliunaite, Roslyn M. Bill |
Editors |
Isabelle Mus-Veteau |
Abstract |
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 Ca(2+)-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. |
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