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.
Additional Comments
NIH grant #: AI101823
NSUWorks Citation
de Azevedo Souza, Clarice; Kristian L. Richards; YoSon Park; Michael Schwartz; Julie Torruellas Garcia; Sara Schesser Bartra; and Gregory V. Plano. 2018. "The YscE/YscG Chaperone and YscF N-Terminal sequences Target YscF to the Yersinia pestis Type III Secretion Apparatus." Microbiology 164, (3): 1-11. doi:10.1099/mic.0.000610.
DOI
10.1099/mic.0.000610
Comments
©2018 The Authors