Gene Symbol: tatE
Description: TatABCE protein translocation system subunit
Alias: ECK0620, JW0622, ybeC
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Eimer E, Fröbel J, Blümmel A, Müller M. TatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases. J Biol Chem. 2015;290:29281-9 pubmed publisher
    ..It is not understood why some bacteria, in addition, constitutively express a functional paralog of TatA called TatE. Here we show, in live Escherichia coli cells, that, upon expression of a Tat substrate protein, fluorescently ..
  2. Hatzixanthis K, Palmer T, Sargent F. A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase. Mol Microbiol. 2003;49:1377-90 pubmed
    ..It is proposed that the mechanism of membrane integration of proteins by the Tat system is fundamentally distinct from that employed for other bacterial inner membrane proteins...
  3. DeLisa M, Tullman D, Georgiou G. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc Natl Acad Sci U S A. 2003;100:6115-20 pubmed
    ..The ability to export proteins with disulfide bonds and the folding proofing feature of the Tat pathway are of interest for biotechnology applications. ..
  4. Dibden D, Green J. In vivo cycling of the Escherichia coli transcription factor FNR between active and inactive states. Microbiology. 2005;151:4063-70 pubmed
    ..The abundance of the FNR- and oxygen-independent tatE transcript was unaffected by changes in oxygen availability...
  5. Jack R, Sargent F, Berks B, Sawers G, Palmer T. Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth. J Bacteriol. 2001;183:1801-4 pubmed
    The transcription start sites for the tatABCD and tatE loci, encoding components of the Tat (twin-arginine translocase) protein export pathway, have been identified...
  6. Thomas J, Daniel R, Errington J, Robinson C. Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli. Mol Microbiol. 2001;39:47-53 pubmed
    ..These data also show for the first time that heterologous proteins can be exported in an active form by the Tat pathway. ..
  7. Wu L, Ize B, Chanal A, Quentin Y, Fichant G. Bacterial twin-arginine signal peptide-dependent protein translocation pathway: evolution and mechanism. J Mol Microbiol Biotechnol. 2000;2:179-89 pubmed
    ..Tat systems show a substrate-Tat component specificity and a species specificity. The pore size of the Tat channel is estimated as being between 5 and 9 nm. Operational models of the Tat system are proposed. ..
  8. Chanal A, Santini C, Wu L. Potential receptor function of three homologous components, TatA, TatB and TatE, of the twin-arginine signal sequence-dependent metalloenzyme translocation pathway in Escherichia coli. Mol Microbiol. 1998;30:674-6 pubmed
  9. Marrichi M, Camacho L, Russell D, DeLisa M. Genetic toggling of alkaline phosphatase folding reveals signal peptides for all major modes of transport across the inner membrane of bacteria. J Biol Chem. 2008;283:35223-35 pubmed publisher

More Information


  1. Sargent F, Gohlke U, De Leeuw E, Stanley N, Palmer T, Saibil H, et al. Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure. Eur J Biochem. 2001;268:3361-7 pubmed
    ..The genes tatA, tatB, tatC and tatE code for integral membrane proteins that are components of the Tat pathway...
  2. Blaudeck N, Kreutzenbeck P, Muller M, Sprenger G, Freudl R. Isolation and characterization of bifunctional Escherichia coli TatA mutant proteins that allow efficient tat-dependent protein translocation in the absence of TatB. J Biol Chem. 2005;280:3426-32 pubmed
    ..Four genes (tatA, tatB, tatC, and tatE) have been identified that encode the components of the E. coli Tat translocation apparatus...
  3. Berthelmann F, Brüser T. Localization of the Tat translocon components in Escherichia coli. FEBS Lett. 2004;569:82-8 pubmed
    ..We suggest that the active translocon complexes are mainly present at polar positions in Escherichia coli. ..
  4. Martin F. Documentation tips to help you stay out of court. Nursing. 1994;24:63-4 pubmed
  5. Sanders C, Wethkamp N, Lill H. Transport of cytochrome c derivatives by the bacterial Tat protein translocation system. Mol Microbiol. 2001;41:241-6 pubmed
    ..We conclude that, in addition to the nature of the specific signal peptide, the folding state of a particular protein also governs its acceptance by a given transport system. ..
  6. Weiner J, Bilous P, Shaw G, Lubitz S, Frost L, Thomas G, et al. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell. 1998;93:93-101 pubmed
    ..MttA, B, and C are members of a large family of related sequences extending from archaebacteria to higher eukaryotes. ..
  7. Bolhuis A, Mathers J, Thomas J, Barrett C, Robinson C. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J Biol Chem. 2001;276:20213-9 pubmed
    ..Co-immunoprecipitation experiments show that TatC is required for the interaction of TatA with TatB, suggesting that TatA may interact with the complex via binding to TatC. ..
  8. Matos C, Robinson C, Di Cola A. The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules. EMBO J. 2008;27:2055-63 pubmed publisher
  9. Sargent F, Bogsch E, Stanley N, Wexler M, Robinson C, Berks B, et al. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 1998;17:3640-50 pubmed
    ..homologues is encoded by the first gene of a four cistron operon, tatABCD, and the second by an unlinked gene, tatE. A mutation previously assigned to the hcf106 homologue encoded at the tatABCD locus, mttA, lies instead in the ..
  10. Tarry M, Schäfer E, Chen S, Buchanan G, Greene N, Lea S, et al. Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. Proc Natl Acad Sci U S A. 2009;106:13284-9 pubmed publisher
    ..Similar TatBC-substrate complexes can be generated by an alternative in vitro reconstitution method and using a different substrate protein. ..
  11. Muller M, Klösgen R. The Tat pathway in bacteria and chloroplasts (review). Mol Membr Biol. 2005;22:113-21 pubmed
    ..Current evidence suggests that a functional Tat translocase is assembled from separate TatBC and TatA assemblies only on demand, i.e., in the presence of transport substrate and a transmembrane H+-motive force. ..
  12. Ize B, G rard F, Zhang M, Chanal A, Voulhoux R, Palmer T, et al. In vivo dissection of the Tat translocation pathway in Escherichia coli. J Mol Biol. 2002;317:327-35 pubmed publisher
    ..In addition to TatE and TatC proteins, either TatA or TatB was sufficient for the translocation of RR-ColV or KR-ColV...
  13. Santini C, Bernadac A, Zhang M, Chanal A, Ize B, Blanco C, et al. Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock. J Biol Chem. 2001;276:8159-64 pubmed
    ..These results strongly suggest a relocalization of periplasmic substances in response to environmental changes. The polar area might be the preferential zone where bacteria sense the change in the environment. ..
  14. Ize B, Stanley N, Buchanan G, Palmer T. Role of the Escherichia coli Tat pathway in outer membrane integrity. Mol Microbiol. 2003;48:1183-93 pubmed
    ..The presence of genes encoding amidases with twin-arginine signal sequences in the genomes of other Gram-negative bacteria suggests that a similar cell envelope defect may be a common feature of tat mutant strains. ..
  15. Beloin C, Valle J, Latour Lambert P, Faure P, Kzreminski M, Balestrino D, et al. Global impact of mature biofilm lifestyle on Escherichia coli K-12 gene expression. Mol Microbiol. 2004;51:659-74 pubmed
    ..These results constitute a comprehensive analysis of the global transcriptional response triggered in mature E. coli biofilms and provide insights into its physiological signature. ..
  16. Penfold D, Sargent F, Macaskie L. Inactivation of the Escherichia coli K-12 twin-arginine translocation system promotes increased hydrogen production. FEMS Microbiol Lett. 2006;262:135-7 pubmed
  17. De Leeuw E, Porcelli I, Sargent F, Palmer T, Berks B. Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. FEBS Lett. 2001;506:143-8 pubmed
    ..The presence of such homo-oligomeric interactions is supported by size exclusion chromatography. ..
  18. Hayden M, Huang I, Bussiere D, Ashley G. The biosynthesis of lipoic acid. Cloning of lip, a lipoate biosynthetic locus of Escherichia coli. J Biol Chem. 1992;267:9512-5 pubmed
    ..A small open reading frame located immediately downstream of the lip gene codes for a small protein of unknown function. ..
  19. Berks B, Sargent F, De Leeuw E, Hinsley A, Stanley N, Jack R, et al. A novel protein transport system involved in the biogenesis of bacterial electron transfer chains. Biochim Biophys Acta. 2000;1459:325-30 pubmed
    ..Here we review the operation of the bacterial Tat system and propose a model for the structural organisation of the Tat preprotein translocase. ..
  20. Berks B, Sargent F, Palmer T. The Tat protein export pathway. Mol Microbiol. 2000;35:260-74 pubmed
    ..Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway. ..
  21. Mould R, Robinson C. A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane. J Biol Chem. 1991;266:12189-93 pubmed
    ..These results indicate that the transport of these proteins across the thylakoid membrane requires a protonmotive force and that the dominant component in this respect is the proton gradient and not the electrical potential. ..
  22. Robinson C, Bolhuis A. Tat-dependent protein targeting in prokaryotes and chloroplasts. Biochim Biophys Acta. 2004;1694:135-47 pubmed
    ..Although the article is focused primarily on bacterial systems, we incorporate relevant aspects of plant thylakoid Tat work and we discuss how the plant and bacterial systems may differ in some respects. ..
  23. Fisher A, DeLisa M. A little help from my friends: quality control of presecretory proteins in bacteria. J Bacteriol. 2004;186:7467-73 pubmed
  24. Bronstein P, Marrichi M, DeLisa M. Dissecting the twin-arginine translocation pathway using genome-wide analysis. Res Microbiol. 2004;155:803-10 pubmed
  25. Yahr T, Wickner W. Functional reconstitution of bacterial Tat translocation in vitro. EMBO J. 2001;20:2472-9 pubmed
    ..The development of an in vitro translocation assay is a prerequisite for further biochemical investigations of the mechanism of translocation, substrate recognition and translocase structure. ..
  26. Wexler M, Sargent F, Jack R, Stanley N, Bogsch E, Robinson C, et al. TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export. J Biol Chem. 2000;275:16717-22 pubmed
    ..TatD is shown to be a cytoplasmic protein. TatD binds to immobilized Ni(2+) or Zn(2+) affinity columns and exhibits magnesium-dependent DNase activity. Features of the tatA operon that may control TatD expression are discussed. ..
  27. Bogsch E, Sargent F, Stanley N, Berks B, Robinson C, Palmer T. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J Biol Chem. 1998;273:18003-6 pubmed
    ..These findings suggest a central role for TatC-type proteins in the translocation of tightly folded proteins across a spectrum of biological membranes. ..