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- W1991671418 abstract "The bacterial twin-arginine translocation (Tat) pathway has the unique ability toexport pre-folded proteins across the cytoplasmic membrane. Its name came from thealmost invariant twin-arginine motif in the signal peptide of Tat substrates.Escherichia coli, a Gram-negative bacterium, is typically used to understand Tatfunction in bacteria. Until now, evidence has shown that TatA, TatB and TatCcomprise the minimally functional unit, moreover, a quality control system exists tomonitor the assembly of cofactors and the correctly folding state of proteins whichavoids the futile export and initiates the degradation of rejected molecules.The research presented in this thesis sought to gain insight into the quality controlmechanism of the Tat pathway in E. coli, and also study the relationship betweentransport and maturation of substrates.In the first place, a novel Tat substrate, YedY, was used to analyse the nature andvariety of proofreading functions operating in conjunction with the Tat pathway. Thesingle substitutions in three predicted ligands for the YedY molybdopterin centre ledto complete inhibition of export and variable degradation of mutated YedY forms,indicating an effective proofreading activity. Circular dichroism spectroscopy andinductively coupled plasma mass spectrometry of purified proteins demonstrated thechange of secondary structures between YedY and mutated variants, and alsoindicated the content of Mo in molybdopterin cofactor within proteins. The datasuggested that the three mutated forms failed to correctly assemble cofactor whichresulted in rejection by the Tat export pathway on the basis of the different changesof secondary structures. Further analysis shows that none of the known exportchaperones for molybdenum cofactor-containing Tat substrates is required for YedYbiogenesis; export is unaffected in cells lacking DmsD and TorD.In the second place, maturation of pre-YedY was blocked when an Ala>Leusubstitution was made at the -1 position of the signal peptide, and a membrane-boundprecursor form accumulated in the membrane. However, the mature domain had beentransferred to the periplasm. The accumulation did not block transport of other Tatsubstrates, indicating the precursor exited from the translocation channel andintegrated into the membrane bilayer. Since the precursor was not detected in theperiplasm, it was suggested that the precursor has undergone lateral transfer into thebilayer during translocation.These results are discussed in relation to the overall mechanism of translocation andproofreading by the Tat pathway in E. coli." @default.
- W1991671418 created "2016-06-24" @default.
- W1991671418 creator A5027505589 @default.
- W1991671418 date "2011-12-01" @default.
- W1991671418 modified "2023-09-23" @default.
- W1991671418 title "The twin arginine translocation pathway in Escherichia coli : mechanism and quality control" @default.
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