Speaker
Mr
Benjamin Brocco
(UJF)
Description
In bacteria, up to 30% of all proteins are translocated into or through the bacterial membrane. This mechanism relies on the trimeric SecYEG (translocon) complex, which forms a pore through the membrane and can open laterally in order to integrate trans-membrane protein into the lipid bilayer1. The energy required to perform the translocation is provided either by the ribosome (co-translational pathway) or the secA ATPase (post-translational pathway)2.
Four additional subunits can join the core translocon :
• Sec D and Sec F favor the translocation by using the proton-motive force3
• YidC, a conserved membrane protein insertase
• YajC, a small protein whose function remains unknown.
This seven-subunit membrane complex is called the holotranslocon (HTL). It is thought to interact with the ribosome and secA and is more efficient for membrane protein integration.
A flexible lipid cavity has been described at the center of the holotranslocon (Botte et al., in revision). We are now investigating its function and dynamic.
Primary author
Mr
Benjamin Brocco
(UJF)
