TatD is a central component of a Tat translocon‐initiated quality control system for exported FeS proteins in <i>Escherichia coli</i>

Matos, Cristina F.R.O.; Cola, Alessandra Di; Robinson, Colin

doi:10.1038/embor.2009.34

Cited by 23 publications

(33 citation statements)

References 22 publications

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“…Neither TatD nor its paralogs has any effect on the secretion of proteins by Tat pathway (267). However, another study found a role for TatD in quality control of FeS proteins that are translocated by the Tat pathway, promoting rapid turnover of misfolded substrates (178), a property difficult to reconcile with proposed nuclease activity of the protein. TatD mutants of E. coli have been reported to exhibit a two-fold increase in the number of constitutive RecA-GFP foci visualized in growing, a property shared by mutants of other 3′ exonucleases such as Exonucleases III, VII, and X (31).…”

Section: E Coli Exonucleases: Properties Structure and Functionmentioning

confidence: 99%

The DNA Exonucleases of Escherichia coli

Lovett

2011

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DNA exonucleases, enzymes that hydrolyze phosphodiester bonds in DNA from a free end, play important cellular roles in DNA repair, genetic recombination and mutation avoidance in all organisms. This article reviews the structure, biochemistry and biological functions of the 17 exonucleases currently identified in the bacterium Escherichia coli. These include the exonucleases associated with DNA polymerases I (polA), II (polB) and III (dnaQ/mutD), Exonucleases I (xonA/sbcB), III (xthA), IV, VII (xseAB), IX (xni/xgdG) and X (exoX), the RecBCD, RecJ, and RecE exonucleases, SbcCD endo/exonuclease, the DNA exonuclease activities of RNase T (rnt) and Endonuclease IV (nfo) and TatD. These enzymes are diverse in terms of substrate specificity and biochemical properties and have specialized biological roles. Most of these enzymes fall into structural families with characteristic sequence motifs, and members of many of these families can be found in all domains of life.

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Section: E Coli Exonucleases: Properties Structure and Functionmentioning

confidence: 99%

The DNA Exonucleases of Escherichia coli

Lovett

2011

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“…Harvested cells were resuspended in 1 mL of chilled buffer (to give a D 600 nm of 10) containing 100 mM Tris/acetate (pH 8.2), 0.5 M sucrose, and 5 mM EDTA. Forty microlitres of lysozyme (2 mgÁmL À1 ) and 500 lL of ice-cold H 2 O were added before incubation on ice for 5 min, and this [36] was followed by the addition of 5 mM MgSO 4 . The spheroplasts were pelleted by centrifugation for 2 min at 20 800 g (Eppendorf 5417R), and the supernatant was collected as the periplasmic fraction.…”

Section: Fractionation Of E Coli Cellsmentioning

confidence: 99%

High‐level secretion of a recombinant protein to the culture medium with a Bacillus subtilis twin‐arginine translocation system in Escherichia coli

et al. 2013

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The twin‐arginine translocation (Tat) system transports folded proteins across the plasma membrane in bacteria, and heterologous proteins can be exported by this pathway if a Tat‐type signal peptide is present at the N‐terminus. The system thus has potential for biopharmaceutical production in Escherichia coli, where export to the periplasm is often a favoured approach. Previous studies have shown that E. coli cells can export high levels of protein by the Tat pathway, and the protein product accummulates almost exclusively in the periplasm. In this study, we analysed E. coli cells that express the Bacillus subtilis TatAdCd system in place of the native TatABC system. We show that a heterologous model protein, comprising the TorA signal peptide linked to green fluorescent protein (TorA–GFP), is efficiently exported by the TatAdCd system. However, whereas the GFP is exported initially to the periplasm during batch fermentation, the mature protein is increasingly found in the extracellular culture medium. By the end of a 16‐h fermentation, ~ 90% of exported GFP is present in the medium as active mature protein. The total protein profiles of the medium and periplasm are essentially identical, confirming that the outer membrane becomes leaky during the fermentation process. The cells are otherwise intact, and there is no large‐scale release of cytoplasmic contents. Export levels are relatively high, with ~ 0.35 g GFP·L−1 culture present in the medium. This system thus offers a means of producing recombinant protein in E. coli and harvesting directly from the medium, with potential advantages in terms of ease of purification and downstream processing.

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“…coli lacking all TatD paralogues is not impaired in Tat-dependent protein export [41]. Although TatD of E. coli was reported to be required for the degradation of translocation-incompetent, malfolded Tat substrates in vivo [78], this effect was not seen under normal expression levels of the RR-precursor [79]. Consistent with its ubiquitous occurrence, TatD has frequently been characterized as a deoxyribonuclease with no obvious functional link to the Tat pathway [41,80,81].…”

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

confidence: 82%

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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TatD is a central component of a Tat translocon‐initiated quality control system for exported FeS proteins in Escherichia coli

Cited by 23 publications

References 22 publications

The DNA Exonucleases of Escherichia coli

The DNA Exonucleases of Escherichia coli

High‐level secretion of a recombinant protein to the culture medium with a Bacillus subtilis twin‐arginine translocation system in Escherichia coli

Twin-arginine-dependent translocation of folded proteins

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