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Getting a grip on non‐native proteins
Author(s) -
Stirling Peter C,
Lundin Victor F,
Leroux Michel R
Publication year - 2003
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.embor869
Subject(s) - native state , protein folding , protein aggregation , co chaperone , function (biology) , membrane protein , biology , microbiology and biotechnology , chemistry , biochemistry , membrane , heat shock protein , gene , hsp90
It is an underappreciated fact that non‐native polypeptides are prevalent in the cellular environment. Native proteins have the folded structure, assembled state and cellular localization required for activity. By contrast, non‐native proteins lack function and are particularly prone to aggregation because hydrophobic residues that are normally buried are exposed on their surfaces. These unstable entities include polypeptides that are undergoing synthesis, transport to and translocation across membranes, and those that are unfolded before degradation. Non‐native proteins are normal, biologically relevant components of a healthy cell, except in cases in which their misfolding results from disease‐causing mutations or adverse extrinsic factors. Here, we explore the nature and occurrence of non‐native proteins, and describe the diverse families of molecular chaperones and coordinated cellular responses that have evolved to prevent their misfolding and aggregation, thereby maintaining quality control over these potentially damaging protein species.