Open AccessThe multitalented type III chaperones: all you can do with 15 kDa
Author(s) -
Feldman Mario F,
Cornelis Guy R
Publication year - 2003
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00042-9
Subject(s) - chaperone (clinical) , co chaperone , secretion , type (biology) , transcription (linguistics) , protein family , biology , microbiology and biotechnology , computational biology , hierarchy , transcription factor , chemical chaperone , chemistry , genetics , biochemistry , unfolded protein response , gene , hsp90 , medicine , endoplasmic reticulum , heat shock protein , ecology , linguistics , philosophy , pathology , economics , market economy
Despite the fact that type III chaperones were discovered approximately 10 years ago, the precise role of most of them is still mysterious. A panoply of functions has been proposed for the members of this family of proteins. Type III chaperones have been suggested to act as anti‐aggregation and stabilizing factors. They have also been proposed to keep their substrates in unfolded or partially folded structures, set a hierarchy on secretion, and participate in the regulation of the transcription of the type III substrates. Here, we review this enigmatic family of proteins, and discuss the experimental data supporting the roles proposed for type III chaperones.