Signal sequence-dependent assembly of Tat translocon subunits (P13)

• Subject Area: Cell Biology
• Term: from 2007 to 2018
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 26068018

Transporting proteins across cellular membranes is a vital process. Most transported proteins pass in an unfolded conformation through proteinaceous structures (translocons). In contrast, the bacterial twin-arginine translocon (Tat) translocates fully folded proteins, some of which representing virulence factors. Without compromising the membrane barrier, the Tat translocon forms a transient conduit of unknown structure from four membrane proteins (TatA,B,C,E). By reconstituting the purified TatABCE proteins into transport-competent proteoliposomes and by employing measures to arrest the transport event, the composition of a functional Tat translocon will be elucidated.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 746: Functional Specificity by Coupling and Modification of Proteins
• Applicant Institution: Albert-Ludwigs-Universität Freiburg
• Project Head: Professor Dr. Matthias Müller