Membrane Protein Production in the Yeast P. pastoris.

Autor:	Ayub H; Faculty of Health and Life Sciences, Coventry University, Coventry, UK., Clare M; Faculty of Health and Life Sciences, Coventry University, Coventry, UK., Broadbent L; College of Health and Life Sciences, Aston University, Birmingham, UK., Simms J; College of Health and Life Sciences, Aston University, Birmingham, UK., Goddard AD; College of Health and Life Sciences, Aston University, Birmingham, UK., Rothnie AJ; College of Health and Life Sciences, Aston University, Birmingham, UK., Bill RM; College of Health and Life Sciences, Aston University, Birmingham, UK. r.m.bill@aston.ac.uk.
Jazyk:	angličtina
Zdroj:	Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2022; Vol. 2507, pp. 187-199.
DOI:	10.1007/978-1-0716-2368-8_10
Abstrakt:	The first crystal structures of recombinant mammalian membrane proteins were solved using high-quality protein that had been produced in yeast cells. One of these, the rat Kv1.2 voltage-gated potassium channel, was synthesized in Pichia pastoris. Since then, this yeast species has remained a consistently popular choice of host for synthesizing eukaryotic membrane proteins because it is quick, easy, and cheap to culture and is capable of posttranslational modification. Very recent structures of recombinant membrane proteins produced in P. pastoris include a series of X-ray crystallography structures of the human vitamin K epoxide reductase and a cryo-electron microscopy structure of the TMEM206 proton-activated chloride channel from pufferfish. P. pastoris has also been used to structurally and functionally characterize a range of membrane proteins including tetraspanins, aquaporins, and G protein-coupled receptors. This chapter provides an overview of the methodological approaches underpinning these successes. (© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)
Databáze:	MEDLINE
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