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Membrane Protein Production in the Yeast, S. cerevisiae.
Cartwright, Stephanie P; Mikaliunaite, Lina; Bill, Roslyn M.
Affiliation
  • Cartwright SP; School of Life & Health Sciences, Aston University, Birmingham, B4 7ET, UK.
  • Mikaliunaite L; School of Life & Health Sciences, Aston University, Birmingham, B4 7ET, UK.
  • Bill RM; School of Life & Health Sciences, Aston University, Birmingham, B4 7ET, UK. r.m.bill@aston.ac.uk.
Methods Mol Biol ; 1432: 23-35, 2016.
Article in En | MEDLINE | ID: mdl-27485327
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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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Membrane Proteins Limits: Animals Language: En Journal: Methods Mol Biol Journal subject: BIOLOGIA MOLECULAR Year: 2016 Document type: Article Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Membrane Proteins Limits: Animals Language: En Journal: Methods Mol Biol Journal subject: BIOLOGIA MOLECULAR Year: 2016 Document type: Article Country of publication: United States