Structure and Dynamics of the Central Lipid Pool and Proteins of the Bacterial Holo-Translocon

Remy Martin, Andreas Haahr Larsen, Robin Adam Corey, Søren Roi Midtgaard, Henrich Frielinghaus, Christiane Schaffitzel, Lise Arleth*, Ian Collinson

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

5 Citations (Scopus)
231 Downloads (Pure)

Abstract

The bacterial Sec translocon, SecYEG, associates with accessory proteins YidC and the SecDF-YajC subcomplex to form the bacterial holo-translocon (HTL). The HTL is a dynamic and flexible protein transport machine capable of coordinating protein secretion across the membrane and efficient lateral insertion of nascent membrane proteins. It has been hypothesized that a central lipid core facilitates the controlled passage of membrane proteins into the bilayer, ensuring the efficient formation of their native state. By performing small-angle neutron scattering on protein solubilized in “match-out” deuterated detergent, we have been able to interrogate a “naked” HTL complex, with the scattering contribution of the surrounding detergent micelle rendered invisible. Such an approach has allowed the confirmation of a lipid core within the HTL, which accommodates between 8 and 29 lipids. Coarse-grained molecular dynamics simulations of the HTL also demonstrate a dynamic, central pool of lipids. An opening at this lipid-rich region between YidC and the SecY lateral gate may provide an exit gateway for newly synthesized, correctly oriented, membrane protein helices, or even small bundles of helices, to emerge from the HTL.

Original languageEnglish
Pages (from-to)1931-1940
Number of pages10
JournalBiophysical Journal
Volume116
Issue number10
Early online date9 Apr 2019
DOIs
Publication statusPublished - 21 May 2019

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