TY  - BOOK
AU  - Fröbel,J.
AU  - Rose,P.
AU  - Müller,M.
TI  - Twin-arginine-dependent translocation of folded proteins
KW  - TATA PORE
KW  - TATBC RECEPTOR
KW  - TATA-TYPE PROTEIN
KW  - TATC-TYPE PROTEIN
KW  - PROOFREADING CHAPERONES
KW  - TWIN-ARGININE TRANSLOCATION (TAT)
N2  - 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
UR  - https://drive.google.com/file/d/10uSL36ryLtmNOqF1h9xtgsIjRd__HfU0/view?usp=drivesdk
ER  -