Biology Faculty Articles

Title

The YscE/YscG Chaperone and YscF N-Terminal sequences Target YscF to the Yersinia pestis Type III Secretion Apparatus

Document Type

Article

Publication Date

3-1-2018

Publication Title

Microbiology

Keywords

Yersinia pestis, Plague, Type III secretion, Chaperone, Protein secretion

ISSN

1350-0872

Volume

164

Issue/No.

3

First Page

1

Last Page

11

Abstract

The needle structures of type III secretion (T3S) systems are formed by the secretion and polymerization of a needle subunit protein, YscF in Yersinia pestis. A subset of T3S systems employ unique heterodimeric chaperones, YscE and YscG in Y. pestis, to prevent the polymerization of needle subunits within the bacterial cell. We demonstrate that the YscE/YscG chaperone is also required for stable YscF expression and for secretion of YscF. Overexpression of a functional maltose-binding protein (MBP)–YscG hybrid protein stabilized cytoplasmic YscF but YscF was not secreted in the absence of YscE. Furthermore, a YscE mutant protein was identified that functioned with YscG to stabilize cytosolic YscF; however, YscF was not secreted. These findings confirm a role for the YscE/YscG chaperone in YscF secretion and suggest that YscE may have a specific role in this process. Recent studies have shown that YscF deleted of its N-terminal 15 residues is still secreted and functional, suggesting that YscF may not require an N-terminal secretion signal. However, we demonstrate that YscF contains an N-terminal secretion signal and that a functional N-terminal signal is required for YscF secretion.

Comments

©2018 The Authors

Additional Comments

NIH grant #: AI101823

DOI

10.1099/mic.0.000610

Peer Reviewed

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