Amino acid substitutions influencing intracellular protein folding pathways

FEBS Letters

Mitraki, Anna¹  King, Jonathan¹ 

[1] Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA

关键词: Protein folding in vivo;    Global suppressors;    Phage P22 tailspike;    Inclusion body;   

DOI  :  10.1016/0014-5793(92)80894-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Though an increasing variety of chaperonins are emerging as important factors in directing polypeptide chain folding off the ribosome, the primary amino acid sequence remains the major determinant of final conformation. The ability to identify cytoplasmic folding intermediates in the formation of the tailspike endorhamnosidase of phage P22 has made it possible to isolate two classes of mutations influencing folding intermediates — temperature-sensitive folding mutations and global suppressors of tsf mutants. These and related amino acid substitutions in eukaryotic proteins are discussed in the context of inclusion body formation and problems in the recovery of correctly folded proteins.

【 授权许可】

Unknown