Journal
FEMS MICROBIOLOGY LETTERS
Volume 219, Issue 2, Pages 151-158Publisher
OXFORD UNIV PRESS
DOI: 10.1016/S0378-1097(03)00042-9
Keywords
type III secretion; chaperones; bacterial pathogenesis; Yersinia; SycE
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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. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
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