Topology and Organization of the Type III Secretion Needle Complex Components

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The correct organization of single subunits of multi-protein machines in a three dimensional context is critical for their functionality. Type III secretion systems (T3SS) are molecular machines with the capacity to deliver bacterial effector proteins into host cells and are fundamental for the biology of many pathogenic or symbiotic bacteria. A central component of T3SSs is the needle complex, a multiprotein structure that mediates the passage of effector proteins through the bacterial envelope. We have used cryo electron microscopy combined with bacterial genetics, site-specific labeling, mutational analysis, chemical derivatization and high-resolution mass spectrometry to generate an experimentally validated topographic map of a Salmonella typhimurium T3SS needle complex. This study provides insights into the organization of this evolutionary highly conserved nanomachinery and is the basis for further functional analysis.

Vyšlo v časopise: Topology and Organization of the Type III Secretion Needle Complex Components. PLoS Pathog 6(4): e32767. doi:10.1371/journal.ppat.1000824
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1000824

Souhrn

Zdroje

1. CianciottoNP

2005 Type II secretion: a protein secretion system for all seasons. Trends Microbiol 13 581 588

2. JohnsonTL

AbendrothJ

HolWG

SandkvistM

2006 Type II secretion: from structure to function. FEMS Microbiol Lett 255 175 186

3. LlosaM

RoyC

DehioC

2009 Bacterial type IV secretion systems in human disease. Mol Microbiol 73 141 151

4. FillouxA

HachaniA

BlevesS

2008 The bacterial type VI secretion machine: yet another player for protein transport across membranes. Microbiology 154 1570 1583

5. GalanJE

Wolf-WatzH

2006 Protein delivery into eukaryotic cells by type III secretion machines. Nature 444 567 573

6. KuboriT

1998 Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science 280 602 665

7. SekiyaK

2001 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 11638 11643

8. BlockerA

2001 Structure and composition of the Shigella flexneri “needle complex”, a part of its type III secreton. Mol Microbiol 39 652 663

9. MarlovitsTC

2004 Structural insights into the assembly of the type III secretion needle complex. Science (New York, NY) 306 1040 1042

10. SukhanA

KuboriT

WilsonJ

GalanJE

2001 Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex. J Bacteriol 183 1159 1167

11. MarlovitsTC

2006 Assembly of the inner rod determines needle length in the type III secretion injectisome. Nature 441 637 640

12. SukhanA

KuboriT

GalanJE

2003 Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ. J Bacteriol 185 3480 343

13. CrepinVF

2005 Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein EscJ. Mol Microbiol 55 1658 1670

14. YipCK

2005 Structural characterization of the molecular platform for type III secretion system assembly. Nature 435 702 707

15. SpreterT

2009 A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system. Nat Struct Mol Biol 16 468 476

16. HodgkinsonJL

2009 Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout. Nat Struct Mol Biol 16 477 485

17. HardieKR

LoryS

PugsleyAP

1996 Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J 15 978 988

18. KosterM

1997 The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol Microbiol 26 789 797

19. CollinsRF

DavidsenL

DerrickJP

FordRC

TonjumT

2001 Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure. Journal of Bacteriology 183 3825 3832

20. LinderothNA

SimonMN

RusselM

1997 The filamentous phage pIV multimer visualized by scanning transmission electron microscopy. Science 278 1635 1638

21. ChamiM

2005 Structural Insights into the Secretin PulD and Its Trypsin-resistant Core. J Biol Chem 280 37732 37741

22. KanigaK

BossioJC

GalanJE

1994 The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins. Mol Microbiol 13 555 568

23. KimbroughTG

MillerSI