INSTITUTO DE PROCESOS BIOTECNOLOGICOS Y QUIMICOS ROSARIO
Unidad Ejecutora - UE
congresos y reuniones científicas
Molecular mechanism of protein transport via the Twin-Arginine Translocon (Tat)
FERNANDA BERTONI; TOMAS SUBILS; RODRIGUEZ FERNANDA
Congreso; XLVIII Reunión Anual SAB; 2019
The twin-arginine translocation (Tat) pathway has the remarkable ability of translocating folded proteins across membranes. The Tat pathway is found in bacteria, archaea and plant chloroplasts, and is required for important bacterial cellular processes including respiratory and photosynthetic energy metabolism, cell division, cell motility, quorum sensing, heavy metal resistance, iron acquisition, and biofilm formation. In Escherichia coli the Tat translocon consists of three membrane proteins: TatA, TatB and TatC. In Bacilllus subtilis it only has two components: TatA and TatC. Experimental evidence suggests that a TatBC complex binds to the signal peptide of the substrate protein. This binding event triggers the assembly of TatA with the TatBC-substrate complex, and the substrate protein is then translocated probably via TatA. The Tat pathway appears to employ a unique mechanism to allow the passage of structured substrates without losing the membrane impermeability to ions. How this is achieved by the translocon is not clear. Here we report molecular and structural studies of Tat components aimed at unveiling their molecular mechanism of action.