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Elsevier, Journal of Biological Chemistry, 23(288), p. 16295-16307, 2013

DOI: 10.1074/jbc.m112.446583

Elsevier, Journal of Biological Chemistry, 23(290), p. 14492, 2015

DOI: 10.1074/jbc.a112.446583

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YidC Occupies the Lateral Gate of the SecYEG Translocon and Is Sequentially Displaced by a Nascent Membrane Protein*

Journal article published in 2013 by Ilie Sachelaru, Narcis Adrian Petriman, Renuka Kudva, Patrick Kuhn, Thomas Welte ORCID, Bettina Knapp, Friedel Drepper, Bettina Warscheid, Hans-Georg Koch
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.