@article{mbs:/content/journal/micro/10.1099/mic.0.000610, author = "Souza, Clarice de Azevedo and Richards, Kristian L. and Park, YoSon and Schwartz, Michael and Torruellas Garcia, Julie and Schesser Bartra, Sara and Plano, Gregory V.", title = "The YscE/YscG chaperone and YscF N-terminal sequences target YscF to the Yersinia pestis type III secretion apparatus", journal= "Microbiology", year = "2018", volume = "164", number = "3", pages = "338-348", doi = "https://doi.org/10.1099/mic.0.000610", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.000610", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "protein secretion", keywords = "plague", keywords = "chaperone", keywords = "Yersinia pestis", keywords = "type III secretion", 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.", }