New insight into the molecular mechanisms of two-partner secretion

Trends in Microbiology

Volumn 15, Issue 11, 2007, Pages 508-515

  Mazar, Joseph ^a   Cotter, Peggy A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CHANNEL FORMING BETA BARREL TRANSPORTER PROTEIN; EXOPROTEIN; UNCLASSIFIED DRUG;

ANIMAL; CARBOXY TERMINAL SEQUENCE; CELL SURFACE; FUNGUS; GRAM NEGATIVE BACTERIUM; MACROMOLECULE; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN SECRETION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; REVIEW; TWO PARTNER SECRETION;

AMINO ACID SEQUENCE; BACTERIAL OUTER MEMBRANE PROTEINS; GRAM-NEGATIVE BACTERIA; MEMBRANE TRANSPORT PROTEINS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT;

ANIMALIA; BACTERIA (MICROORGANISMS); FUNGI; NEGIBACTERIA;

EID: 36048935998     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2007.10.005     Document Type: Review

References (53)

1. Aoki S.K., et al. Contact-dependent inhibition of growth in Escherichia coli. Science 309 (2005) 1245-1248
2. Henderson I.R., et al. Type V protein secretion pathway: the autotransporter story. Microbiol. Mol. Biol. Rev. 68 (2004) 692-744
3. Jacob-Dubuisson F., et al. Protein secretion through autotransporter and two-partner pathways. Biochim. Biophys. Acta 1694 (2004) 235-257
4. Yen M.R., et al. Protein-translocating outer membrane porins of Gram-negative bacteria. Biochim. Biophys. Acta 1562 (2002) 6-31
5. Jacob-Dubuisson F., et al. Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins. Mol. Microbiol. 40 (2001) 306-313
6. Kajava A.V., and Steven A.C. The turn of the screw: variations of the abundant beta-solenoid motif in passenger domains of Type V secretory proteins. J. Struct. Biol. 155 (2006) 306-315
7. Genevrois S., et al. The Omp85 protein of Neisseria meningitidis is required for lipid export to the outer membrane. EMBO J. 22 (2003) 1780-1789
8. Voulhoux R., et al. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299 (2003) 262-265
9. Wu T., et al. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121 (2005) 235-245
10. Wu T., et al. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 11754-11759
11. Gentle I., et al. The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria. J. Cell Biol. 164 (2004) 19-24
12. Kozjak V., et al. An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane. J. Biol. Chem. 278 (2003) 48520-48523
13. Reumann S., et al. Evolution of the general protein import pathway of plastids (review). Mol. Membr. Biol. 22 (2005) 73-86
14. Jacob-Dubuisson F., et al. Channel formation by FhaC, the outer membrane protein involved in the secretion of the Bordetella pertussis filamentous hemagglutinin. J. Biol. Chem. 274 (1999) 37731-37735
15. Konninger U.W., et al. The haemolysin-secreting ShlB protein of the outer membrane of Serratia marcescens: determination of surface-exposed residues and formation of ion-permeable pores by ShlB mutants in artificial lipid bilayer membranes. Mol. Microbiol. 32 (1999) 1212-1225
16. Surana N.K., et al. Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 14497-14502
17. Bredemeier R., et al. Functional and phylogenetic properties of the pore-forming beta-barrel transporters of the Omp85 family. J. Biol. Chem. 282 (2007) 1882-1890
18. Guedin S., et al. Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin. J. Biol. Chem. 275 (2000) 30202-30210
19. Ertel F., et al. The evolutionarily related beta-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains. J. Biol. Chem. 280 (2005) 28281-28289
20. Paschen S.A., et al. Evolutionary conservation of biogenesis of beta-barrel membrane proteins. Nature 426 (2003) 862-866
21. Reumann S., et al. The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: identification of a cyanobacterial homolog. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 784-789
22. Reumann S., and Keegstra K. The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes. Trends Plant Sci. 4 (1999) 302-307
23. Moslavac S., et al. Conserved pore-forming regions in polypeptide-transporting proteins. FEBS J. 272 (2005) 1367-1378
24. Sanchez-Pulido L., et al. POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. Trends Biochem. Sci. 28 (2003) 523-526
25. Habib S.J., et al. The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial {beta}-barrel proteins. J. Cell Biol. 176 (2007) 77-88
26. Stegmeier J.F., and Andersen C. Characterization of pores formed by YaeT (Omp85) from Escherichia coli. J. Biochem. (Tokyo) 140 (2006) 275-283
27. Werner J., and Misra R. YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol. Microbiol. 57 (2005) 1450-1459
28. Surana N.K., et al. Translocator proteins in the two-partner secretion family have multiple domains. J. Biol. Chem. 281 (2006) 18051-18058
29. Meli A.C., et al. Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore. J. Biol. Chem. 281 (2006) 158-166
30. Jacob-Dubuisson F., et al. Lack of functional complementation between Bordetella pertussis filamentous hemagglutinin and Proteus mirabilis HpmA hemolysin secretion machineries. J. Bacteriol. 179 (1997) 775-783
31. Jacob-Dubuisson F., et al. Amino-terminal maturation of the Bordetella pertussis filamentous haemagglutinin. Mol. Microbiol. 19 (1996) 65-78
32. Grass S., and St Geme III J.W. Maturation and secretion of the non-typable Haemophilus influenzae HMW1 adhesin: roles of the N-terminal and C-terminal domains. Mol. Microbiol. 36 (2000) 55-67
33. Schonherr R., et al. Amino acid replacements in the Serratia marcescens haemolysin ShIA define sites involved in activation and secretion. Mol. Microbiol. 9 (1993) 1229-1237
34. Clantin B., et al. The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 6194-6199
35. Hodak H., et al. Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate. Mol. Microbiol. 61 (2006) 368-382
36. St Geme III J.W., and Grass S. Secretion of the Haemophilus influenzae HMW1 and HMW2 adhesins involves a periplasmic intermediate and requires the HMWB and HMWC proteins. Mol. Microbiol. 27 (1998) 617-630
37. St Geme III J.W., et al. High-molecular-weight proteins of nontypable Haemophilus influenzae mediate attachment to human epithelial cells. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 2875-2879
38. Buscher A.Z., et al. Surface anchoring of a bacterial adhesin secreted by the two-partner secretion pathway. Mol. Microbiol. 61 (2006) 470-483
39. Dawid S., et al. Mapping of binding domains of nontypeable Haemophilus influenzae HMW1 and HMW2 adhesins. Infect. Immun. 69 (2001) 307-314
40. Cotter P.A., et al. Filamentous hemagglutinin of Bordetella bronchiseptica is required for efficient establishment of tracheal colonization. Infect. Immun. 66 (1998) 5921-5929
41. Relman D.A., et al. Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 2637-2641
42. Chevalier N., et al. Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide. J. Mol. Microbiol. Biotechnol. 8 (2004) 7-18
43. Lambert-Buisine C., et al. N-terminal characterization of the Bordetella pertussis filamentous haemagglutinin. Mol. Microbiol. 28 (1998) 1283-1293
44. Coutte L., et al. Surface anchoring of bacterial subtilisin important for maturation function. Mol. Microbiol. 49 (2003) 529-539
45. Mazar J., and Cotter P.A. Topology and maturation of filamentous haemagglutinin suggest a new model for two-partner secretion. Mol. Microbiol. 62 (2006) 641-654
46. Coutte L., et al. Subtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway. EMBO J. 20 (2001) 5040-5048
47. Kajava A.V., et al. Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins. Mol. Microbiol. 42 (2001) 279-292
48. Makhov A.M., et al. Filamentous hemagglutinin of Bordetella pertussis. A bacterial adhesin formed as a 50-nm monomeric rigid rod based on a 19-residue repeat motif rich in beta strands and turns. J. Mol. Biol. 241 (1994) 110-124
49. Pohlner J., et al. Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. Nature 325 (1987) 458-462
50. Hirono I., et al. Iron-regulated haemolysin gene from Edwardsiella tarda. Mol. Microbiol. 24 (1997) 851-856
51. Ward C.K., et al. Haemophilus ducreyi secretes a filamentous hemagglutinin-like protein. J. Bacteriol. 180 (1998) 6013-6022
52. Renauld-Mongenie G., et al. Distinct roles of the N-terminal and C-terminal precursor domains in the biogenesis of the Bordetella pertussis filamentous hemagglutinin. J. Bacteriol. 178 (1996) 1053-1060
53. Baker D., et al. The role of pro regions in protein folding. Curr. Opin. Cell Biol. 5 (1993) 966-970