Proteomics

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The SecYEG interactome of E. coli: non-competitive binding of PpiD and YidC to the SecYEG translocon


ABSTRACT: The SecYEG translocon constitutes the major protein transporting channel in bacteria and transports an enormous variety of different secretory and inner membrane proteins. The minimal core of the SecYEG translocon consists of the three inner membrane proteins SecY, SecE and SecG, which together with appropriate targeting factors are sufficient for protein transport in vitro. However, in vivo the SecYEG translocon has been shown to associate with multiple partner proteins, which likely allow the SecYEG translocon to manage diverse substrates. For obtaining a global view on SecYEG plasticity, a label free proteomics approach was executed, which identified known SecYEG interacting proteins, verified the interaction with quality control proteins and identified several novel putative SecYEG interactors. Surprisingly, the chaperone complex PpiD/YfgM was identified as the most pronounced contact partner of SecYEG and was much dominant than the established partner protein YidC. Detailed analyses of the PpiD and YidC contact sites on SecY by site directed cross-linking revealed that PpiD and YidC use almost completely overlapping binding sites on SecY and contact the lateral gate, the plug domain and the periplasmic cavity of SecY. Still, despite having almost identical binding sites, their binding to SecY is non-competitive as determined by quantitative mass spectrometry and cross-linking. This implies that the SecYEG translocon forms different substrate-independent sub-assemblies, in which SecYEG is either in contact with YidC or with the PpiD/YfgM complex.

INSTRUMENT(S): LTQ FT

ORGANISM(S): Escherichia coli  

TISSUE(S): Tissue Not Applicable To Dataset

DISEASE(S): Not Available

SUBMITTER: Friedel Drepper  

LAB HEAD: Bettina Warscheid

PROVIDER: PXD015974 | Pride | 2019-11-07

REPOSITORIES: pride

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Publications

Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in Escherichia coli.

Jauss Benjamin B   Petriman Narcis-Adrian NA   Drepper Friedel F   Franz Lisa L   Sachelaru Ilie I   Welte Thomas T   Steinberg Ruth R   Warscheid Bettina B   Koch Hans-Georg HG  

The Journal of biological chemistry 20191107 50


The SecYEG translocon constitutes the major protein transport channel in bacteria and transfers an enormous variety of different secretory and inner-membrane proteins. The minimal core of the SecYEG translocon consists of three inner-membrane proteins, SecY, SecE, and SecG, which, together with appropriate targeting factors, are sufficient for protein transport in vitro However, in vivo the SecYEG translocon has been shown to associate with multiple partner proteins, likely allowing the SecYEG t  ...[more]

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