The Tat protein export pathway

Berks, Ben C.; Sargent, Frank; Palmer, Tracy

doi:10.1046/j.1365-2958.2000.01719.x

Cited by 537 publications

(509 citation statements)

References 99 publications

(156 reference statements)

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“…This is true of protein translocation whether the protein is in the unfolded state, as in sec-dependent protein translocation, or in the folded state, as occurs in the export of metalloproteins through the Tat pathway of bacteria [1][2][3] . Bacterial toxins such as anthrax are also examples of proteins that translocate across membranes but here a much scaled-down apparatus is employed involving pore-forming subunits 4 .…”

Section: Discussionmentioning

confidence: 99%

The cytotoxic domain of colicin E9 is a channel-forming endonuclease

et al. 2002

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Article:Mosbahi, Khédidja, Lemaître, Christelle, Mobasheri, Hamid et al. (6 more authors) (2002) The cytotoxic domain of colicin E9 is a channel-forming endonuclease. Nature Structural Biology. pp. 476-484. ISSN 1545-9985 https://doi.org/10.1038/nsb797 eprints@whiterose.ac.uk https://eprints.whiterose.ac.uk/ Reuse Items deposited in White Rose Research Online are protected by copyright, with all rights reserved unless indicated otherwise. They may be downloaded and/or printed for private study, or other acts as permitted by national copyright laws. The publisher or other rights holders may allow further reproduction and re-use of the full text version. This is indicated by the licence information on the White Rose Research Online record for the item. TakedownIf you consider content in White Rose Research Online to be in breach of UK law, please notify us by emailing eprints@whiterose.ac.uk including the URL of the record and the reason for the withdrawal request. White Rose Consortium ePrints Repositoryhttp://eprints.whiterose.ac.uk/ This is an author produced version of a paper published in Nature Structural Biology. This paper has been peer-reviewed but does not include final publisher proof-corrections or journal pagination.White Rose Repository URL for this paper: http://eprints.whiterose.ac.uk/archive/00001066/ Citation for the published paper Mosbahi, Khédidja and Lemaître, Christelle and Keeble, Anthony H. and Mobasheri, Hamid and Morel, Bertrand and James, Richard and Moore, Geoffrey R. and Lea, Edward J. A. and Kleanthous, Colin (2002) The cytotoxic domain of colicin E9 is a channel-forming endonuclease. Nature Structural Biology, 9 (6). pp. 476-484. Citation for this paperTo refer to the repository paper, the following format may be used: Mosbahi, Khédidja and Lemaître, Christelle and Keeble, Anthony H. and Mobasheri, Hamid and Morel, Bertrand and James, Richard and Moore, Geoffrey R. and Lea, Edward J. A. and Kleanthous, Colin (2002) Colicin E9 is a 60 kDa toxin that is normally released from colicinogenic bacteria in the form of a heterodimeric complex with its 9.5 kDa immunity protein, Im9 (ref. 14). The immunity protein protects the colicin-producing bacterium from the activity of its own toxin but is jettisoned on entry of the colicin into a susceptible cell 15 . Hence, the form of the toxin tested in the bilayer experiments had the immunity protein removed (see Materials andMethods section). Previous work from our laboratory has shown that this form of the toxin retains complete biological activity 14 . Immunity-free colicin E9 (2 nM) was added to the cis chamber of a bilayer apparatus in 10 mM Tris/HCl buffer at pH 7.5, containing 0.1 M NaCl and 10 mM CaCl 2 , and a potential difference (p.d.) applied across the membrane. Random, fluctuating current was observed that showed evidence of opening and closing events with conductance of the order of ~100 pS, although larger conductance states were also seen ( Fig. 1a). In order to identify the region(s) of the protein responsible for this a...

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Section: Discussionmentioning

confidence: 99%

The cytotoxic domain of colicin E9 is a channel-forming endonuclease

et al. 2002

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“…Proteins recognized by the Tat translocation pathway contain a double arginine at their extreme N-termini. These proteins are translocated in a folded state (Berks et al, 2000). It is believed that halobacterial proteins already have to fold in the cytoplasm to circumvent precipitation caused by the high internal salt concentration.…”

Section: Signal Peptidesmentioning

confidence: 99%

Insights into ABC Transport in Archaea

Albers

Koning

Konings

et al. 2004

J Bioenerg Biomembr

101

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In archaea, ATP-binding cassette (ABC) transporters play a crucial role in substrate uptake, export, and osmoregulation. Archaeal substrate-binding-protein-dependent ABC transporters are equipped with a very high affinity for their cognate substrates which provide these organisms with the ability to efficiently scavenge substrates from their environment even when present only at low concentration. Further adaptations to the archaeal way of life are especially found in the domain organization and anchoring of the substrate-binding proteins to the membrane. Examination of the signal peptides of binding proteins of 14 archaeal genomes showed clear differences between euryarchaeotes and crenarchaeotes. Furthermore, a profiling and comparison of ABC transporters in the three sequenced pyrococcal strains was performed.

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“…Nonetheless, it has been known that Yid pathway is involved in the threading mechanism for unfolded proteins only. Furthermore, it was previously unknown whether there existed another folded protein export pathway, in addition to the Tat pathway, that was large enough to allow translocation of the folded protein (Berks et al, 2000). Thus, we concluded that the Yid translocon has a much smaller diameter for transporting the folded GFP with an anchor function and a neutral N-terminal sequence compared with the Sec translocon, showing both blocked and low levels of GFP expression of those with an anchor function sequence and an alkaline N-terminus (Fig.…”

Section: Effect Of N-terminal Pi With An Anchor Function On Gfp Exprementioning

confidence: 99%

Novel GFP Expression Using a Short N-Terminal Polypeptide through the Defined Twin-Arginine Translocation (Tat) Pathway

Lee

Han

Kim

et al. 2011

Molecules and Cells

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Escherichia coli is frequently used as a convenient host organism for soluble recombinant protein expression. However, additional strategies are needed for proteins with complex folding characteristics. Here, we suggested that the acidic, neutral, and alkaline isoelectric point (pI) range curves correspond to the channels of the E. coli type-II cytoplasmic membrane translocation (periplasmic translocation) pathways of twin-arginine translocation (Tat), Yid, and general secretory pathway (Sec), respectively, for unfolded and folded target proteins by examining the characteristic pI values of the N-termini of the signal sequences or the leader sequences, matching with the known diameter of the translocation channels, and analyzing the N-terminal pI value of the signal sequences of the Tat substrates. To confirm these proposed translocation pathways, we investigated the soluble expression of the folded green fluorescent protein (GFP) with short N-terminal polypeptides exhibiting pI and hydrophilicity separately or collectively. This, in turn, revealed the existence of an anchor function with a specific directionality based on the N-terminal pI value (termed as N-terminal pI-specific directionality) and distinguished the presence of the E. coli type-II cytoplasmic membrane translocation pathways of Tat, Yid, and Sec for the unfolded and folded target proteins. We concluded that the pI value and hydrophilicity of the short N-terminal polypeptide, and the total translational efficiency of the target proteins based on the ΔG RNA value of the N-terminal coding regions are important factors for promoting more efficient translocation (secretion) through the largest diameter of the Tat channel. These results show that the short N-terminal polypeptide could substitute for the Tat signal sequence with improved efficiency.

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The Tat protein export pathway

Cited by 537 publications

References 99 publications

The cytotoxic domain of colicin E9 is a channel-forming endonuclease

The cytotoxic domain of colicin E9 is a channel-forming endonuclease

Insights into ABC Transport in Archaea

Novel GFP Expression Using a Short N-Terminal Polypeptide through the Defined Twin-Arginine Translocation (Tat) Pathway

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