TY - JOUR
T1 - The YscE/YscG chaperone and YscF N-terminal sequences target YscF to the yersinia pestis type III secretion apparatus
AU - Souza, Clarice de Azevedo
AU - Richards, Kristian L.
AU - Park, Yoson
AU - Schwartz, Michael
AU - Torruellas Garcia, Julie
AU - Schesser Bartra, Sara
AU - Plano, Gregory V.
N1 - Funding Information:
This research was supported by a grant from the National Institutes of Health NIH (AI101823). We thank Dr David Waugh for providing the purified YscEFG heterotrimeric complex. C. A. S. and K. R. contributed equally to this manuscript. The molecular graphics were performed with the UCSF Chimera package. Chimera was developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco (supported by NIGMS P41-GM103311).
Funding Information:
This research was supported by a grant from the National Institutes of Health (AI101823).
Publisher Copyright:
© 2018 The Authors.
PY - 2018/3
Y1 - 2018/3
N2 - 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 maltosebinding 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.
AB - 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 maltosebinding 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.
KW - Chaperone
KW - Plague
KW - Protein secretion
KW - Type III secretion
KW - Yersinia pestis
UR - http://www.scopus.com/inward/record.url?scp=85043782723&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85043782723&partnerID=8YFLogxK
U2 - 10.1099/mic.0.000610
DO - 10.1099/mic.0.000610
M3 - Article
C2 - 29458689
AN - SCOPUS:85043782723
VL - 164
SP - 338
EP - 348
JO - Microbiology (United Kingdom)
JF - Microbiology (United Kingdom)
SN - 1350-0872
IS - 3
M1 - 000610
ER -