Type III secretion systems shape up as they ship out

Current Opinion in Microbiology

Volumn 13, Issue 1, 2010, Pages 47-52

  Marlovits, Thomas C ^a,b   Stebbins, C Erec ^c  

^a RESEARCH INSTITUTE OF MOLECULAR PATHOLOGY   (Austria)

^b ERICH SCHMID INSTITUTE OF MATERIALS SCIENCE   (Austria)

^c ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

BACTERIAL VIRULENCE; BIOLOGICAL ACTIVITY; ELECTRON MICROSCOPY; GRAM NEGATIVE BACTERIUM; HOST CELL; MOLECULAR MODEL; NONHUMAN; PROKARYOTE; PROTEIN FUNCTION; PROTEIN STRUCTURE; REVIEW; SEQUENCE HOMOLOGY; TYPE III SECRETION SYSTEM; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; MACROMOLECULAR SUBSTANCES; MEMBRANE TRANSPORT PROTEINS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; PROTEIN BINDING; PROTEIN FOLDING; VIRULENCE FACTORS;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; PROKARYOTA;

EID: 75249090025     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2009.11.001     Document Type: Review

References (41)

1. Galan J.E., and Wolf-Watz H. Protein delivery into eukaryotic cells by type III secretion machines. Nature 444 (2006) 567-573
2. Cornelis G.R. The type III secretion injectisome. Nat Rev Microbiol 4 (2006) 811-825
3. Macnab R.M. How bacteria assemble flagella. Annu Rev Microbiol 57 (2003) 77-100
4. Tampakaki A.P., Fadouloglou V.E., Gazi A.D., Panopoulos N.J., and Kokkinidis M. Conserved features of type III secretion. Cell Microbiol 6 (2004) 805-816
5. Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., et al. Illuminating the evolutionary history of chlamydiae. Science 304 (2004) 728-730
6. Cunnac S., Lindeberg M., and Collmer A. Pseudomonas syringae type III secretion system effectors: repertoires in search of functions. Curr Opin Microbiol 12 (2009) 53-60
7. Parsot C. Shigella type III secretion effectors: how, where, when, for what purposes?. Curr Opin Microbiol 12 (2009) 110-116
8. McGhie E.J., Brawn L.C., Hume P.J., Humphreys D., and Koronakis V. Salmonella takes control: effector-driven manipulation of the host. Curr Opin Microbiol 12 (2009) 117-124
9. Poueymiro M., and Genin S. Secreted proteins from Ralstonia solanacearum: a hundred tricks to kill a plant. Curr Opin Microbiol 12 (2009) 44-52
10. Galan J.E. Common themes in the design and function of bacterial effectors. Cell Host Microbe 5 (2009) 571-579
11. Moraes T.F., Spreter T., and Strynadka N.C. Piecing together the type III injectisome of bacterial pathogens. Curr Opin Struct Biol 18 (2008) 258-266
12. Kubori T., Matsushima Y., Nakamura D., Uralil J., Lara-Tejero M., Sukhan A., Galan J.E., and Aizawa S.I. Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science 280 (1998) 602-605
13. Kimbrough T.G., and Miller S.I. Contribution of Salmonella typhimurium type III secretion components to needle complex formation. Proc Natl Acad Sci U S A 97 (2000) 11008-11013
14. Marlovits T.C., Kubori T., Sukhan A., Thomas D.R., Galan J.E., and Unger V.M. Structural insights into the assembly of the type III secretion needle complex. Science 306 (2004) 1040-1042
15. Marlovits T.C., Kubori T., Lara-Tejero M., Thomas D., Unger V.M., and Galan J.E. Assembly of the inner rod determines needle length in the type III secretion injectisome. Nature 441 (2006) 637-640. This paper presents cryo-electron microscopy of the Salmonella needle complex, revealing for the first time the inner rod assembly and relationship to needle length.
16. Hodgkinson J.L., Horsley A., Stabat D., Simon M., Johnson S., da Fonseca P.C., Morris E.P., Wall J.S., Lea S.M., and Blocker A.J. Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout. Nat Struct Mol Biol 16 (2009) 477-485. The paper presents the most recent electron microscopic data of the Shigella needle complex, arguing for a 12-fold symmetry.
17. Crago A.M., and Koronakis V. Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol Microbiol 30 (1998) 47-56
18. Daefler S., and Russel M. The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG. Mol Microbiol 28 (1998) 1367-1380
19. Lario P.I., Pfuetzner R.A., Frey E.A., Creagh L., Haynes C., Maurelli A.T., and Strynadka N.C. Structure: biochemical analysis of a secretin pilot protein. EMBO J 24 (2005) 1111-1121
20. Zenk S.F., Stabat D., Hodgkinson J.L., Veenendaal A.K., Johnson S., and Blocker A.J. Identification of minor inner-membrane components of the Shigella type III secretion system 'needle complex'. Microbiology 153 (2007) 2405-2415
21. Sekiya K., Ohishi M., Ogino T., Tamano K., Sasakawa C., and Abe A. Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure. Proc Natl Acad Sci U S A 98 (2001) 11638-11643
22. Ogino T., Ohno R., Sekiya K., Kuwae A., Matsuzawa T., Nonaka T., Fukuda H., Imajoh-Ohmi S., and Abe A. Assembly of the type III secretion apparatus of enteropathogenic Escherichia coli. J Bacteriol 188 (2006) 2801-2811
23. Mueller C.A., Broz P., and Cornelis G.R. The type III secretion system tip complex and translocon. Mol Microbiol 68 (2008) 1085-1095
24. Akeda Y., and Galan J.E. Chaperone release and unfolding of substrates in type III secretion. Nature 437 (2005) 911-915
25. Hensel M., Shea J.E., Gleeson C., Jones M.D., Dalton E., and Holden D.W. Simultaneous identification of bacterial virulence genes by negative selection. Science 269 (1995) 400-403
26. Li J., Ochman H., Groisman E.A., Boyd E.F., Solomon F., Nelson K., and Selander R.K. Relationship between evolutionary rate and cellular location among the Inv/Spa invasion proteins of Salmonella enterica. Proc Natl Acad Sci U S A 92 (1995) 7252-7256
27. Macnab R.M. Type III flagellar protein export and flagellar assembly. Biochim Biophys Acta 1694 (2004) 207-217
28. Muller S.A., Pozidis C., Stone R., Meesters C., Chami M., Engel A., Economou A., and Stahlberg H. Double hexameric ring assembly of the type III protein translocase ATPase HrcN. Mol Microbiol 61 (2006) 119-125
29. Zarivach R., Vuckovic M., Deng W., Finlay B.B., and Strynadka N.C. Structural analysis of a prototypical ATPase from the type III secretion system. Nat Struct Mol Biol 14 (2007) 131-137
30. Zarivach R., Deng W., Vuckovic M., Felise H.B., Nguyen H.V., Miller S.I., Finlay B.B., and Strynadka N.C. Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS. Nature 453 (2008) 124-127
31. Blocker A., Jouihri N., Larquet E., Gounon P., Ebel F., Parsot C., Sansonetti P., and Allaoui A. Structure and composition of the Shigella flexneri "needle complex", a part of its type III secreton. Mol Microbiol 39 (2001) 652-663
32. Chami M., Guilvout I., Gregorini M., Remigy H.W., Muller S.A., Valerio M., Engel A., Pugsley A.P., and Bayan N. Structural insights into the secretin PulD and its trypsin-resistant core. J Biol Chem 280 (2005) 37732-37741
33. Wood S.E., Jin J., and Lloyd S.A. YscP, YscU switch the substrate specificity of the Yersinia type III secretion system by regulating export of the inner rod protein YscI. J Bacteriol 190 (2008) 4252-4262
34. Yip C.K., Kimbrough T.G., Felise H.B., Vuckovic M., Thomas N.A., Pfuetzner R.A., Frey E.A., Finlay B.B., Miller S.I., and Strynadka N.C. Structural characterization of the molecular platform for type III secretion system assembly. Nature 435 (2005) 702-707
35. Spreter T., Yip C.K., Sanowar S., Andre I., Kimbrough T.G., Vuckovic M., Pfuetzner R.A., Deng W., Yu A.C., Finlay B.B., et al. A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system. Nat Struct Mol Biol 16 (2009) 468-476. This paper presents crytallographic structures of several elements of the basal body, revealing conserved features, and presents fitting of the structures into EM density.
36. Korotkov K.V., Pardon E., Steyaert J., and Hol W.G. Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 17 (2009) 255-265
37. Opalka N., Beckmann R., Boisset N., Simon M.N., Russel M., and Darst S.A. Structure of the filamentous phage pIV multimer by cryo-electron microscopy. J Mol Biol 325 (2003) 461-470
38. Collins R.F., Frye S.A., Kitmitto A., Ford R.C., Tonjum T., and Derrick J.P. Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 Å resolution. J Biol Chem 279 (2004) 39750-39756
39. Burghout P., van Boxtel R., Van Gelder P., Ringler P., Muller S.A., Tommassen J., and Koster M. Structure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica. J Bacteriol 186 (2004) 4645-4654
40. Valverde R., Edwards L., and Regan L. Structure and function of KH domains. FEBS J 275 (2008) 2712-2726
41. Mishima M., Shida T., Yabuki K., Kato K., Sekiguchi J., and Kojima C. Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR. Biochemistry 44 (2005) 10153-10163