02248nam a2200265Ia 4500 MX-MdCICY 20260521091417.0 CICY B-14331 Twin-arginine-dependent translocation of folded proteins Phil. Trans. R. Soc., 367(1592), p.1029-1046, 2012 Twin-arginine translocation (Tat)denotes a protein transport pathway in bacteria, archaea and plant chloroplasts, which is specific for precursor proteins harbouring a characteristic twin-arginine pair in their signal sequences. Many Tat substrates receive cofactors and fold prior to translocation. For a subset of them, proofreading chaperones coordinate maturation and membrane-targeting. Tat translocases comprise two kinds of membrane proteins, a hexahelical TatC-type protein and one or two members of the single-spanning TatA protein family, called TatA and TatB. TatC- and TatAtype proteins form homo- and hetero-oligomeric complexes. The subunits of TatABC translocases are predominantly recovered from two separate complexes, a TatBC complex that might contain some TatA, and a homomeric TatA complex. TatB and TatC coordinately recognize twin-arginine signal peptides and accommodate them in membrane-embedded binding pockets. Advanced binding of the signal sequence to the Tat translocase requires the proton-motive force (PMF)across the membranes and might involve a first recruitment of TatA. When targeted in this manner, folded twin-arginine precursors induce homo-oligomerization of TatB and TatA. Ultimately, this leads to the formation of a transmembrane protein conduit that possibly consists of a pore-like TatA structure. The translocation step again is dependent on the PMF. TATA PORE TATBC RECEPTOR TATA-TYPE PROTEIN TATC-TYPE PROTEIN PROOFREADING CHAPERONES TWIN-ARGININE TRANSLOCATION (TAT) Fröbel, J. Rose, P. Müller, M. https://drive.google.com/file/d/10uSL36ryLtmNOqF1h9xtgsIjRd__HfU0/view?usp=drivesdk Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx Loc REF1 250602s9999 xx |||||s2 |||| ||und|d 24464 24464 0 0 Loc 0 0 F1 CICY CICY RE 2025-06-25 0 B-14331 2025-06-25 15:39:39 2025-06-25 REF1