The multitalented type III chaperones: All you can do with 15 kDa

Mario F. Feldman; Guy R. Cornelis

doi:10.1016/S0378-1097(03)00042-9

The multitalented type III chaperones: All you can do with 15 kDa

Mario F. Feldman
, Guy R. Cornelis

Research output: Contribution to journal › Short survey › peer-review

124 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	151-158
Number of pages	8
Journal	FEMS Microbiology Letters
Volume	219
Issue number	2
DOIs	https://doi.org/10.1016/S0378-1097(03)00042-9
State	Published - Feb 28 2003

Keywords

Bacterial pathogenesis
Chaperones
SycE
Type III secretion
Yersinia

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10.1016/S0378-1097(03)00042-9

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title = "The multitalented type III chaperones: All you can do with 15 kDa",

abstract = "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.",

keywords = "Bacterial pathogenesis, Chaperones, SycE, Type III secretion, Yersinia",

author = "Feldman, \{Mario F.\} and Cornelis, \{Guy R.\}",

note = "Funding Information: We thank Jaime Mota and Paul Troisfontaines for the critical reading of the manuscript and Trui Denecker for the help in the design of the figures. The laboratory is supported by the Swiss National Science Foundation (Grant 32-65393.01), the Belgian {\textquoteleft}Fonds National de la Recherche Scientifique M{\'e}dicale{\textquoteright} (Convention 3.4595.97), the Belgian {\textquoteleft}Direction g{\'e}n{\'e}rale de la Recherche Scientifique Communaut{\'e} Fran{\c c}aise de Belgique{\textquoteright} (Action de Recherche Concert{\'e}e 94/99-172). The laboratory also participates in the EU TMR network {\textquoteleft}MEMBMACS{\textquoteright} (contract HRPN-CT-2000-00075).",

year = "2003",

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doi = "10.1016/S0378-1097(03)00042-9",

language = "English",

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TY - JOUR

T1 - The multitalented type III chaperones

T2 - All you can do with 15 kDa

AU - Feldman, Mario F.

AU - Cornelis, Guy R.

N1 - Funding Information: We thank Jaime Mota and Paul Troisfontaines for the critical reading of the manuscript and Trui Denecker for the help in the design of the figures. The laboratory is supported by the Swiss National Science Foundation (Grant 32-65393.01), the Belgian ‘Fonds National de la Recherche Scientifique Médicale’ (Convention 3.4595.97), the Belgian ‘Direction générale de la Recherche Scientifique Communauté Française de Belgique’ (Action de Recherche Concertée 94/99-172). The laboratory also participates in the EU TMR network ‘MEMBMACS’ (contract HRPN-CT-2000-00075).

PY - 2003/2/28

Y1 - 2003/2/28

N2 - 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.

AB - 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.

KW - Bacterial pathogenesis

KW - Chaperones

KW - SycE

KW - Type III secretion

KW - Yersinia

UR - https://www.scopus.com/pages/publications/0037469577

U2 - 10.1016/S0378-1097(03)00042-9

DO - 10.1016/S0378-1097(03)00042-9

M3 - Short survey

C2 - 12620614

AN - SCOPUS:0037469577

SN - 0378-1097

VL - 219

SP - 151

EP - 158

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 2

ER -

The multitalented type III chaperones: All you can do with 15 kDa

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Keywords

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