Proteomics

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SseF-SscB Interaction - Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems

ABSTRACT: Bacterial type III secretion systems are able to secrete membrane proteins. In this project we could show that cognate T3SS chaperones are able to bind to the transmembrane segments of T3SS substrates to avoid erroneous targeting to the bacterial inner membrane. Here, we studied the Salmonella SPI-2 T3SS secreted protein SseF and the interaction with its chaperone SscB by in vivo photocrosslinking. LC-MS/MS analysis was done to provide additional evidence that SscB is the interaction partner leading to the upshift of the SseF band in an SDS-PAGE analysis.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Salmonella Enterica Subsp. Enterica Serovar Typhimurium

SUBMITTER: Nicolas Nalpas  

LAB HEAD: Samuel Wagner

PROVIDER: PXD010470 | Pride | 2018-10-16

REPOSITORIES: Pride

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Publications

Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems.

Krampen Lea L   Malmsheimer Silke S   Grin Iwan I   Trunk Thomas T   Lührmann Anja A   de Gier Jan-Willem JW   Wagner Samuel S  

Nature communications 20180827 1

Many bacteria export effector proteins fulfilling their function in membranes of a eukaryotic host. These effector membrane proteins appear to contain signals for two incompatible bacterial secretion pathways in the same protein: a specific export signal, as well as transmembrane segments that one would expect to mediate targeting to the bacterial inner membrane. Here, we show that the transmembrane segments of effector proteins of type III and type IV secretion systems indeed integrate in the m  ...[more]

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