%0 Journal Article %1 petrimanInteractionNetworkYidC2018 %A Petriman, Narcis-Adrian %A Jauß, Benjamin %A Hufnagel, Antonia %A Franz, Lisa %A Sachelaru, Ilie %A Drepper, Friedel %A Warscheid, Bettina %A Koch, Hans-Georg %C England %D 2018 %J Scientific reports %K Bacterial Binding,Protein Channels/metabolism,to_read Conformation,Receptors Cytoplasmic Molecular,Protein Nuclear/metabolism,SEC Proteins/*chemistry/*metabolism,Models Proteins/chemistry/*metabolism,Escherichia Proteins/metabolism,Binding Sites,Escherichia Translocation Transport and coli coli/*metabolism,Membrane %N 1 %P 578 %R 10.1038/s41598-017-19019-w %T The Interaction Network of the YidC Insertase with the SecYEG Translocon, SRP and the SRP Receptor FtsY. %V 8 %X YidC/Oxa1/Alb3 are essential proteins that operate independently or cooperatively with the Sec machinery during membrane protein insertion in bacteria, archaea and eukaryotic organelles. Although the interaction between the bacterial SecYEG translocon and YidC has been observed in multiple studies, it is still unknown which domains of YidC are in contact with the SecYEG translocon. By in vivo and in vitro site-directed and para-formaldehyde cross-linking we identified the auxiliary transmembrane domain 1 of E. coli YidC as a major contact site for SecY and SecG. Additional SecY contacts were observed for the tightly packed globular domain and the C1 loop of YidC, which reveals that the hydrophilic cavity of YidC faces the lateral gate of SecY. Surprisingly, YidC-SecYEG contacts were only observed when YidC and SecYEG were present at about stoichiometric concentrations, suggesting that the YidC-SecYEG contact in vivo is either very transient or only observed for a very small SecYEG sub-population. This is different for the YidC-SRP and YidC-FtsY interaction, which involves the C1 loop of YidC and is efficiently observed even at sub-stoichiometric concentrations of SRP/FtsY. In summary, our data provide a first detailed view on how YidC interacts with the SecYEG translocon and the SRP-targeting machinery.

@article{petrimanInteractionNetworkYidC2018, abstract = {YidC/Oxa1/Alb3 are essential proteins that operate independently or cooperatively with the Sec machinery during membrane protein insertion in bacteria, archaea and eukaryotic organelles. Although the interaction between the bacterial SecYEG translocon and YidC has been observed in multiple studies, it is still unknown which domains of YidC are in contact with the SecYEG translocon. By in vivo and in vitro site-directed and para-formaldehyde cross-linking we identified the auxiliary transmembrane domain 1 of E. coli YidC as a major contact site for SecY and SecG. Additional SecY contacts were observed for the tightly packed globular domain and the C1 loop of YidC, which reveals that the hydrophilic cavity of YidC faces the lateral gate of SecY. Surprisingly, YidC-SecYEG contacts were only observed when YidC and SecYEG were present at about stoichiometric concentrations, suggesting that the YidC-SecYEG contact in vivo is either very transient or only observed for a very small SecYEG sub-population. This is different for the YidC-SRP and YidC-FtsY interaction, which involves the C1 loop of YidC and is efficiently observed even at sub-stoichiometric concentrations of SRP/FtsY. In summary, our data provide a first detailed view on how YidC interacts with the SecYEG translocon and the SRP-targeting machinery.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {England}, author = {Petriman, Narcis-Adrian and Jau{\ss}, Benjamin and Hufnagel, Antonia and Franz, Lisa and Sachelaru, Ilie and Drepper, Friedel and Warscheid, Bettina and Koch, Hans-Georg}, biburl = {https://www.bibsonomy.org/bibtex/21eb6452d1323e643b7aa3fbd4f9abd85/warscheidlab}, doi = {10.1038/s41598-017-19019-w}, interhash = {ac21a66114184a5fc2dbfeff0e7c29b6}, intrahash = {1eb6452d1323e643b7aa3fbd4f9abd85}, issn = {2045-2322}, journal = {Scientific reports}, keywords = {Bacterial Binding,Protein Channels/metabolism,to_read Conformation,Receptors Cytoplasmic Molecular,Protein Nuclear/metabolism,SEC Proteins/*chemistry/*metabolism,Models Proteins/chemistry/*metabolism,Escherichia Proteins/metabolism,Binding Sites,Escherichia Translocation Transport and coli coli/*metabolism,Membrane}, langid = {english}, month = jan, number = 1, pages = 578, pmcid = {PMC5766551}, pmid = {29330529}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {The Interaction Network of the {{YidC}} Insertase with the {{SecYEG}} Translocon, {{SRP}} and the {{SRP}} Receptor {{FtsY}}.}, volume = 8, year = 2018 }