Consensus structural features of purified bacterial TatABC complexes

Journal of Molecular Biology

Volumn 330, Issue 2, 2003, Pages 277-286

  Oates, Joanne ^a   Mathers, Joanne ^a   Mangels, Dorothea ^a   Kühlbrandt, Werner ^b   Robinson, Colin ^a,c   Model, Kirstin ^b  

^a UNIVERSITY OF WARWICK   (United Kingdom)

^b MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^c UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Membrane protein complexes; Protein transport; Tat system; TorA; Twin arginine signal peptide

Indexed keywords

CARRIER PROTEIN; OXIDOREDUCTASE; TRIMETHYLAMINE OXIDE; TWIN ARGININE TRANSLOCATION A PROTEIN; TWIN ARGININE TRANSLOCATION B PROTEIN; TWIN ARGININE TRANSLOCATION C PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL MEMBRANE; BACTERIAL STRAIN; COMPLEX FORMATION; CONTROLLED STUDY; ELECTRON MICROSCOPY; ESCHERICHIA COLI; GENE EXPRESSION; GENETIC CONSERVATION; MEMBRANE TRANSPORT; MUTANT; NONHUMAN; OPERON; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; RHIZOBIUM RADIOBACTER; SALMONELLA TYPHIMURIUM; SEQUENCE HOMOLOGY; STAINING;

AGROBACTERIUM; AGROBACTERIUM TUMEFACIENS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; SALMONELLA TYPHIMURIUM;

EID: 0038122836     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00621-1     Document Type: Article

References (41)

1. Robinson C., Bolhuis A. Protein targeting by the twin-arginine translocation pathway. Nature Rev. Mol. Cell. Biol. 2:2001;350-355.
2. Dalbey R.E., Kuhn A. Evolutionarily related insertion pathways of bacterial, mitochondrial, and thylakoid membrane proteins. Annu. Rev. Cell. Dev. Biol. 16:2000;51-87.
3. Chaddock A.M., Mant A., Karnauchov I., Brink S., Herrmann R.G., Klösgen R.B., Robinson C. A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the ΔpH-dependent thylakoidal protein translocase. EMBO J. 14:1995;2715-2722.
4. Stanley N.R., Palmer T., Berks B.C. The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 275:2000;11591-11596.
5. Brink S., Bogsch E.G., Edwards W.R., Hynds P.J., Robinson C. Targeting of thylakoid proteins by the ΔpH-driven twin-arginine translocation pathway requires a specific signal in the hydrophobic domain in conjunction with the twin-arginine motif. FEBS Letters. 434:1998;425-430.
6. Cristobal S., de Gier J.W., Nielsen H., von Heijne G. Competition between Sec- and TAT-dependent protein translocation in Escherichia coli. EMBO J. 18:1999;2982-2990.
7. Clark S.A., Theg S.M. A folded protein can be transported across the chloroplast envelope and thylakoid membranes. Mol. Biol. Cell. 8:1997;923-934.
8. Hynds P., Robinson D., Robinson C. The Sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane. J. Biol. Chem. 273:1998;34868-34874.
9. Berks B. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22:1996;393-404.
10. Santini C., Ize B., Chanal A., Müller M., Giordano G., Wu L.F. A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17:1998;101-112.
11. 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. 93:1998;93-101.
12. Sargent F., Bogsch E., Stanley N., Wexler M., Robinson C., Berks B., Palmer T. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17:1998;3640-3650.
13. 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. 273:1998;18003-18006.
14. Yen M.R., Tseng Y.H., Nguyen E.H., Wu L.F., Saier M.H. Jr. Sequence and phylogenetic analyzes of the twin-arginine targeting (Tat) protein export system. Arch. Microbiol. 177:2002;441-450.
15. Bolhuis A., Mathers J.E., Thomas J.D., Barrett C.M.L., Robinson C. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J. Biol. Chem. 276:2001;20213-20219.
16. Gouffi K., Santini C.L., Wu L.F. Topology determination and functional analysis of the Escherichia coli TatC protein. FEBS Letters. 525:2002;65-70.
17. Cline K., Mori H. Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport. J. Cell Biol. 154:2001;719-729.
18. Mori H., Cline K. A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid Delta pH/Tat translocase. J. Cell Biol. 157:2002;205-210.
19. Allen S.C.H., Barrett C.M.L., Ray N., Robinson C. Essential cytoplasmic domains in the Escherichia coli TatC protein. J. Biol. Chem. 277:2002;10362-10366.
20. Buchanan G., De Leeuw E., Stanley N.R., Wexler M., Berks B.C., Sargent F., Palmer T. Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis. Mol. Microbiol. 43:2002;1457-1470.
21. Porcelli I., de Leeuw E., Wallis R., van den Brink-van der Laan E., de Kruijff B., Wallace B.A., et al. Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system. Biochemistry. 41:2002;13690-13697.
22. Ding Z., Christie P.J. Agrobacterium tumefaciens twin-arginine-dependent translocation is important for virulence, flagellation, and chemotaxis but not type IV secretion. J. Bacteriol. 185:2003;760-771.
23. Diday E. Introduction to dynamic clusters method (Dyc Program). Metra. 11:1972;505-515.
24. Halbig D., Wiegert T., Blaudeck N., Freudl R., Sprenger G.A. The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding. Eur. J. Biochem. 263:1999;543-551.
25. Blaudeck N., Sprenger G.A., Freudl R., Wiegert T. Specificity of signal peptide recognition in tat-dependent bacterial protein translocation. J Bacteriol. 183:2001;604-610.
26. Veenhoff L.M., Heuberger E., Poolman B. Quaternary structure and function of transport proteins. Trends Biochem. Sci. 27:2002;242-249.
27. Sargent F., Stanley N.R., Berks B.C., Palmer T. Sec-independent protein translocation in Escherichia coli - a distinct and pivotal role for the TatB protein. J. Biol. Chem. 274:1999;36073-36082.
28. De Leeuw E., Granjon T., Porcelli I., Alami M., Carr S., Müller M., et al. Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. J. Mol. Biol. 322:2002;1135-1146.
29. Sargent F., Gohlke U., de Leeuw E., Stanley N.R., Palmer T., Saibil H.R., Berks B.C. Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure. Eur. J. Biochem. 268:2001;3361-3367.
30. Casadaban M.J., Cohen S.N. Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences. Proc. Natl Acad. Sci. USA. 76:1979;4530-4533.
31. Wexler M., Sargent F., Jack R.L., Stanley N.R., Bogsch E.G., 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. 275:2000;16717-16722.
32. Bolhuis A., Bogsch E.G., Robinson C. Subunit interactions in the twin-arginine translocase complex of Escherichia coli. FEBS Letters. 472:2000;88-92.
33. Thomas J.D., Daniel R.A., 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. 39:2001;47-52.
34. BAD promoter. J. Bacteriol. 177:1995;4121-4130.
35. Model K., Prinz T., Ruiz T., Radermacher M., Krimmer T., Kühlbrandt W., et al. Protein translocase of the outer mitochondrial membrane: role of import receptors in the structural organization of the TOM complex. J. Mol. Biol. 316:2002;657-666.
36. Radermacher M., Ruiz T., Wieczorek H., Grüber G. The structure of the V-1-ATPase determined by three-dimensional electron microscopy of single particles. J. Struct. Biol. 135:2001;26-37.
37. Frank J., Radermacher M., Penczek P., Zhu J., Li Y.H., Ladjadj M., Leith A., SPIDER E.B. Processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116:1996;190-199.
38. Marco S., Chagoyen M., de la Fraga L.G., Carazo J.M., Carrascosa J.L. A variant to the "random approximation" of the reference-free alignment algorithm. Ultramicroscopy. 66:1996;5-12.
39. van Heel M., Frank J. Use of multivariate statistics in analysing the images of biological macromolecules. Ultramicroscopy. 6:1981;187-196.
40. Marabini R., Carazo J.M. Pattern recognition and classification of images of biological macromolecules using artificial neural networks. Biophys. J. 66:1994;1804-1814.
41. Saxton W.O., Baumeister W. The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsc. 127:1982;127-138.