Structure of TatA Paralog, TatE, Suggests a Structurally Homogeneous Form of Tat Protein Translocase That Transports Folded Proteins of Differing Diameter

Baglieri, Jacopo; Beck, Daniel; Vasisht, N.; Smith, Corinne J.; Robinson, Colin

doi:10.1074/jbc.m111.326355

Cited by 34 publications

(38 citation statements)

References 40 publications

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“…TatA and TatE (a TatA paralog) form ring-like oligomers in detergent (12,18,25) (Fig. S2A), consistent with diffusion measurements of fluorescent TatA complexes in cell membranes (16).…”

Section: Discussionsupporting

confidence: 80%

“…S2A), consistent with diffusion measurements of fluorescent TatA complexes in cell membranes (16). The precise oligomeric state of TatA is variable in cell membranes (16) and detergent micelles (12,18,25). At low concentrations of DPC, TatA adopts an average oligomer size of approximately 9, which is smaller than that of TatA in C 12 E 9 (18) and digitonin (12) but comparable to that of TatE in dodecylmaltoside (25).…”

Section: Discussionsupporting

confidence: 74%

“…Although the oligomer state may represent a range of oligomers rather than a single oligomer, the spectral similarities indicate that the TatA protomers adopt highly similar structures and intersubunit relationships. Negative-stain electron microscopy at this DPR shows a ring-like morphology similar to that of TatA or TatE in other detergents (12,18,25) (Fig. S2A).…”

Section: Resultsmentioning

confidence: 76%

“…These conditions make structural studies in membranes extremely difficult. However, solubilization of TatA using mild detergents, such as dodecyl nonaoxyethylene ether (C 12 E 9 ), digitonin, or dodecylmaltoside, favors TatA oligomerization and this manipulation has allowed determination of low-resolution electron microscopy structures of TatA and of TatE, a secondary TatA copy found in E. coli (12,18,25). The electron microscopy structures show ring-like complexes but provide no details of the arrangement of the oligomers within the electron density or knowledge about how TatA is able to mediate transport of folded proteins.…”

mentioning

confidence: 99%

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Structural model for the protein-translocating element of the twin-arginine transport system

Rodriguez

Rouse

Tait

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

102

157

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The twin-arginine translocase (Tat) carries out the remarkable process of translocating fully folded proteins across the cytoplasmic membrane of prokaryotes and the thylakoid membrane of plant chloroplasts. Tat is required for bacterial pathogenesis and for photosynthesis in plants. TatA, the protein-translocating element of the Tat system, is a small transmembrane protein that assembles into ring-like oligomers of variable size. We have determined a structural model of the Escherichia coli TatA complex in detergent solution by NMR. TatA assembly is mediated entirely by the transmembrane helix. The amphipathic helix extends outwards from the ring of transmembrane helices, permitting assembly of complexes with variable subunit numbers. Transmembrane residue Gln8 points inward, resulting in a short hydrophobic pore in the center of the complex. Simulations of the TatA complex in lipid bilayers indicate that the short transmembrane domain distorts the membrane. This finding suggests that TatA facilitates protein transport by sensitizing the membrane to transient rupture.

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“…TatA and TatE (a TatA paralog) form ring-like oligomers in detergent (12,18,25) (Fig. S2A), consistent with diffusion measurements of fluorescent TatA complexes in cell membranes (16).…”

Section: Discussionsupporting

confidence: 80%

Section: Discussionsupporting

confidence: 74%

Section: Resultsmentioning

confidence: 76%

mentioning

confidence: 99%

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Structural model for the protein-translocating element of the twin-arginine transport system

Rodriguez

Rouse

Tait

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

102

157

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“…The concept of size-fitting pores that consist of an appropriate number of TatA monomers was recently challenged by the finding that TatE, the functional paralogue of TatA in E. coli, also forms pore-like structures which, however, are considerably smaller than those of TatA [111].…”

Section: The Components Of Tat Translocases (A) Homologues Of Tatc Anmentioning

confidence: 99%

Twin-arginine-dependent translocation of folded proteins

Fröbel

Rose

Müller

2012

Phil. Trans. R. Soc. B

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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.

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Mapping the twin-arginine protein translocation network ofBacillus subtilis

et al. 2013

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Bacteria employ twin-arginine translocation (Tat) pathways for the transport of folded proteins to extracytoplasmic destinations. In recent years, most studies on bacterial Tat pathways addressed the membrane-bound TatA(B)C subunits of the Tat translocase, and the specific interactions between this translocase and its substrate proteins. In contrast, relatively few studies investigated possible coactors in the TatA(B)C-dependent protein translocation process. The present studies were aimed at identifying interaction partners of the Tat pathway of Bacillus subtilis, which is a paradigm for studies on protein secretion by Gram-positive bacteria. Specifically, 36 interaction partners of the TatA and TatC subunits were identified by rigorous application of the yeast two-hybrid (Y2H) approach. Our Y2H analyses revealed that the three TatA isoforms of B. subtilis can form homo- and heterodimers. Subsequently, the secretion of the Tat substrates YwbN and PhoD was tested in mutant strains lacking genes for the TatAC interaction partners identified in our genome-wide Y2H screens. Our results show that the cell wall-bound protease WprA is important for YwbN secretion, and that the HemAT and CsbC proteins are required for PhoD secretion under phosphate starvation conditions. Taken together, our findings imply that the Bacillus Tat pathway is embedded in an intricate protein-protein interaction network.

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Structure of TatA Paralog, TatE, Suggests a Structurally Homogeneous Form of Tat Protein Translocase That Transports Folded Proteins of Differing Diameter

Cited by 34 publications

References 40 publications

Structural model for the protein-translocating element of the twin-arginine transport system

Structural model for the protein-translocating element of the twin-arginine transport system

Twin-arginine-dependent translocation of folded proteins

Mapping the twin-arginine protein translocation network ofBacillus subtilis

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