Advances in the production of membrane proteins in Pichia pastoris

被引:25
作者
Ramon, Ana [1 ]
Marin, Monica [1 ]
机构
[1] Fac Ciencias, Secc Bioquim Biol Mol, Montevideo 11400, Uruguay
关键词
Heterologous protein production; Integral membrane protein; Pichia pastoris; Protein expression; Protein folding; RHIZOPUS-ORYZAE LIPASE; HUMAN SERUM-ALBUMIN; METHYLOTROPHIC YEAST; CRYSTAL-STRUCTURE; K+ CHANNEL; PLASMODIUM-FALCIPARUM; RECOMBINANT PROTEINS; EXPRESSION SYSTEM; STRUCTURAL BASIS; CODON USAGE;
D O I
10.1002/biot.201100146
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Membrane proteins play key roles in diverse cellular functions and have become the target for a large number of pharmacological drugs. Despite representing about 20-30% of cellular proteins, their characterization is long overdue since they are difficult to handle, to purify from their natural source or to obtain as recombinant proteins. Pichia pastoris is a methylotrophic yeast species increasingly used as a host for heterologous protein expression for both research and industrial purposes. Over the past few years many efforts have allowed important advances in the development of this expression system for the expression and production of membrane proteins. The most recent achievements in improving yield and proper folding of integral membrane proteins are summarized in this review.
引用
收藏
页码:700 / 706
页数:7
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