Most membrane proteins are co-translationally inserted into the lipid bilayer via the universally conserved SecY complex and they access the lipid phase presumably via a lateral gate in SecY. In bacteria, the lipid transfer of membrane proteins from the SecY channel is assisted by the SecY-associated protein YidC, but details on the SecY-YidC interaction are unknown. By employing an in vivo and in vitro site-directed cross-linking approach, we have mapped the SecY-YidC interface and found YidC in contact with all four transmembrane domains of the lateral gate. This interaction did not require the SecDFYajC complex and was not influenced by SecA binding to SecY. In contrast, ribosomes dissociated the YidC contacts to lateral gate helices 2b and 8. The major contact between YidC and the lateral gate was lost in the presence of ribosome nascent chains and new SecY-YidC contacts appeared. These data demonstrate that the SecY-YidC interaction is influenced by nascent-membrane-induced lateral gate movements.
%0 Journal Article
%1 sachelaruYidCOccupiesLateral2013
%A Sachelaru, Ilie
%A Petriman, Narcis Adrian
%A Kudva, Renuka
%A Kuhn, Patrick
%A Welte, Thomas
%A Knapp, Bettina
%A Drepper, Friedel
%A Warscheid, Bettina
%A Koch, Hans-Georg
%C United States
%D 2013
%J The Journal of biological chemistry
%K Bilayers/*metabolism,Membrane Binding,Protein Biogenesis,Membrane Channels,Secretion,Signal Escherichia Mapping,Protein Particle,to_read Proteins/genetics/*metabolism,Escherichia Proteins/genetics/*metabolism,Membrane Proteins/genetics/*metabolism,Peptide Recognition Targeting,Protein Trafficking,Membrane Translocation Transport Transport/physiology,SEC coli coli/genetics/*metabolism,Lipid
%N 23
%P 16295--16307
%R 10.1074/jbc.M112.446583
%T YidC Occupies the Lateral Gate of the SecYEG Translocon and Is Sequentially Displaced by a Nascent Membrane Protein.
%V 288
%X Most membrane proteins are co-translationally inserted into the lipid bilayer via the universally conserved SecY complex and they access the lipid phase presumably via a lateral gate in SecY. In bacteria, the lipid transfer of membrane proteins from the SecY channel is assisted by the SecY-associated protein YidC, but details on the SecY-YidC interaction are unknown. By employing an in vivo and in vitro site-directed cross-linking approach, we have mapped the SecY-YidC interface and found YidC in contact with all four transmembrane domains of the lateral gate. This interaction did not require the SecDFYajC complex and was not influenced by SecA binding to SecY. In contrast, ribosomes dissociated the YidC contacts to lateral gate helices 2b and 8. The major contact between YidC and the lateral gate was lost in the presence of ribosome nascent chains and new SecY-YidC contacts appeared. These data demonstrate that the SecY-YidC interaction is influenced by nascent-membrane-induced lateral gate movements.
@article{sachelaruYidCOccupiesLateral2013,
abstract = {Most membrane proteins are co-translationally inserted into the lipid bilayer via the universally conserved SecY complex and they access the lipid phase presumably via a lateral gate in SecY. In bacteria, the lipid transfer of membrane proteins from the SecY channel is assisted by the SecY-associated protein YidC, but details on the SecY-YidC interaction are unknown. By employing an in vivo and in vitro site-directed cross-linking approach, we have mapped the SecY-YidC interface and found YidC in contact with all four transmembrane domains of the lateral gate. This interaction did not require the SecDFYajC complex and was not influenced by SecA binding to SecY. In contrast, ribosomes dissociated the YidC contacts to lateral gate helices 2b and 8. The major contact between YidC and the lateral gate was lost in the presence of ribosome nascent chains and new SecY-YidC contacts appeared. These data demonstrate that the SecY-YidC interaction is influenced by nascent-membrane-induced lateral gate movements.},
added-at = {2024-05-17T13:01:35.000+0200},
address = {United States},
author = {Sachelaru, Ilie and Petriman, Narcis Adrian and Kudva, Renuka and Kuhn, Patrick and Welte, Thomas and Knapp, Bettina and Drepper, Friedel and Warscheid, Bettina and Koch, Hans-Georg},
biburl = {https://www.bibsonomy.org/bibtex/28064ccf0a8824c52ce9d3a63cdadb25a/warscheidlab},
doi = {10.1074/jbc.M112.446583},
interhash = {16f17f6d0a40ea8c190092c49caadaf2},
intrahash = {8064ccf0a8824c52ce9d3a63cdadb25a},
issn = {1083-351X 0021-9258},
journal = {The Journal of biological chemistry},
keywords = {Bilayers/*metabolism,Membrane Binding,Protein Biogenesis,Membrane Channels,Secretion,Signal Escherichia Mapping,Protein Particle,to_read Proteins/genetics/*metabolism,Escherichia Proteins/genetics/*metabolism,Membrane Proteins/genetics/*metabolism,Peptide Recognition Targeting,Protein Trafficking,Membrane Translocation Transport Transport/physiology,SEC coli coli/genetics/*metabolism,Lipid},
langid = {english},
month = jun,
number = 23,
pages = {16295--16307},
pmcid = {PMC3675568},
pmid = {23609445},
timestamp = {2024-05-17T13:01:35.000+0200},
title = {{{YidC}} Occupies the Lateral Gate of the {{SecYEG}} Translocon and Is Sequentially Displaced by a Nascent Membrane Protein.},
volume = 288,
year = 2013
}