Proteomics

Dataset Information

0

Non-competitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in E. coli


ABSTRACT: 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 translocon to process its diverse substrates. To obtain a global view on SecYEG plasticity in Escherichia coli, here we performed a quantitative interaction proteomic analysis, which identified several known SecYEG-interacting proteins, verified the interaction of SecYEG with quality-control proteins, and revealed several previously unknown putative SecYEG interacting proteins. Surprisingly, we found that the chaperone complex PpiD/YfgM is the most prominent interaction partner of SecYEG. Detailed analyses of the PpiD–SecY interaction by site-directed cross-linking revealed that PpiD and the established SecY partner protein YidC use almost completely overlapping binding sites on SecY. Both PpiD and YidC contacted the lateral gate, the plug domain, and the periplasmic cavity of SecY. However, quantitative MS and cross-linking analyses revealed that despite having almost identical binding sites, their binding to SecY is non-competitive. This observation suggests that the SecYEG translocon forms different substrate-independent subassemblies in which SecYEG either associates with YidC or with the PpiD/YfgM complex. In summary, the results of this study indicate that the PpiD/YfgM chaperone complex is a primary interaction partner of the SecYEG translocon.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Escherichia coli  

TISSUE(S): Tissue Not Applicable To Dataset

DISEASE(S): Not Available

SUBMITTER: Friedel Drepper  

LAB HEAD: Bettina Warscheid

PROVIDER: PXD015985 | Pride | 2019-11-07

REPOSITORIES: pride

altmetric image

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]

Similar Datasets

2019-11-07 | PXD015974 | Pride
2022-06-06 | PXD008875 | Pride
2015-01-09 | PXD001210 | Pride
2018-06-04 | PXD009747 | Pride
2012-07-04 | E-GEOD-24852 | ArrayExpress
2015-04-29 | E-GEOD-62102 | ArrayExpress
2019-02-09 | PXD010314 | Pride
2012-05-22 | E-GEOD-25064 | ArrayExpress
2014-07-23 | E-GEOD-59649 | ArrayExpress
2012-07-04 | E-GEOD-24904 | ArrayExpress