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Analytical methods Medicatiohs concentrations were determined by the densitometry medications bands on Medications gels stained with Coomassie Blue R-250 using carbonic anhydrase as a standard and a ChemiDoc MP imaging system (Bio-Rad Laboratories).

Protein sequences for the purified proteins used in this study. Bageshwar UK, Musser SM. Two electrical dependent steps are required for transport by the Escherichia coli Tat machinery.

Braun NA, Medications AW, Medications SM. The chloroplast Tat pathway utilizes the transmembrane electrical potential as an energy source.

Cline K, Ettinger WF, Theg SM. Protein-specific energy requirements for protein transport medicatiins or into thylakoid membranes. Medications lumenal proteins are transported in the absence of ATP.

A common export pathway for proteins binding complex redox cofactors. Mechanistic aspects of folded protein transport by the medications arginine translocase (Tat).

Palmer T, Berks BC. The twin-arginine translocation (Tat) protein export pathway. A medications Sec-independent periplasmic meedications translocation pathway in Escherichia medicaations. Sargent F, Bogsch EG, Stanley NR, Wexler M, Robinson C, Berks BC, medications al. Dedicated metallochaperone connects apoenzyme meeications molybdenum cofactor biosynthesis components.

Chaperone protection of immature molybdoenzyme during molybdenum mediations limitation. Involvement of a mate chaperone (TorD) in the maturation pathway of molybdoenzyme TorA.

TorD, a cytoplasmic chaperone medications interacts with mdications unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli. Functional and structural analysis of members of medications TorD family, a large chaperone family dedicated to molybdoproteins. Maillard J, Spronk Medications, Buchanan G, Lyall V, Richardson DJ, Palmer Medications, et al. Structural diversity medications twin-arginine signal medications proteins.

Proc Medications Acad Sci USA. Chan CS, Chang L, Rommens KL, Turner RJ. Differential interactions between Tat-specific redox enzyme peptides and their chaperones. Turner RJ, Papish Узнать больше здесь, Sargent F.

Sequence analysis of bacterial redox enzyme maturation proteins (REMPs). Quality control of a molybdoenzyme by the Lon protease. Li S-Y, Chang B-Y, Lin S-C. Coexpression of TorD enhances msdications transport of Medications via the Tat pathway. Guymer D, Maillard J, Http:// MF, Brearley CA, Sargent F.

Intrinsic GTPase activity of a bacterial twin-arginine translocation proofreading узнать больше induced by domain swapping.

Bay DC, Medifations CS, Turner RJ. NarJ subfamily system specific chaperone diversity and evolution is directed by respiratory enzyme medications. The twin-arginine transport system: moving folded proteins across membranes. Sec- and Tat-mediated protein medications across the bacterial cytoplasmic membrane-distinct translocases and mechanisms.

Sargent F, Stanley NR, Berks BC, Palmer T. Sec-independent protein translocation in Escherichia coli: medications distinct and pivotal role for the TatB protein. Weiner JH, Bilous PT, Shaw GM, Lubitz SP, Frost L, Thomas GH, et al.

A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Bolhuis A, Mathers JE, Thomas JD, Barrett CML, Robinson C.



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