Dimerization of the pseudomonas aeruginosa translocator chaperone PcrH is required for stability, not function

Journal of Bacteriology

Volumn 195, Issue 21, 2013, Pages 4836-4843

  Tomalka, Amanda G ^a   Zmina, Stephanie E ^a   Stopford, Charles M ^a,b   Rietsch, Arne ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CHAPERONE; FUNGAL PROTEIN; MUTANT PROTEIN; PCRH PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CYTOPLASM; DIMERIZATION; DISSOCIATION; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STABILITY; PSEUDOMONAS AERUGINOSA; TYPE III SECRETION SYSTEM; WILD TYPE; YERSINIA;

BACTERIAL PROTEINS; CARRIER PROTEINS; DIMERIZATION; GENE EXPRESSION REGULATION, BACTERIAL; MOLECULAR CHAPERONES; MUTATION; PROTEIN STABILITY; PROTEIN TRANSPORT; PSEUDOMONAS AERUGINOSA; TWO-HYBRID SYSTEM TECHNIQUES; VIRULENCE;

EID: 84885962359     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00335-13     Document Type: Article

References (24)

1. Troisfontaines P, Cornelis GR. 2005. Type III secretion: more systems than you think. Physiology (Bethesda) 20:326-339.
2. Galan JE, Wolf-Watz H. 2006. Protein delivery into eukaryotic cells by type III secretion machines. Nature 444:567-573.
3. Mueller CA, Broz P, Cornelis GR. 2008. The type III secretion system tip complex and translocon. Mol. Microbiol. 68:1085-1095.
4. Broms JE, Forslund AL, Forsberg A, Francis MS. 2003. PcrH of Pseudomonas aeruginosa is essential for secretion and assembly of the type III translocon. J. Infect. Dis. 188:1909-1921.
5. Schoehn G, Di Guilmi AM, Lemaire D, Attree I, Weissenhorn W, Dessen A. 2003. Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas. EMBO J. 22:4957-4967.
6. Broms JE, Edqvist PJ, Forsberg A, Francis MS. 2006. Tetratricopeptide repeats are essential for PcrH chaperone function in Pseudomonas aeruginosa type III secretion. FEMS Microbiol. Lett. 256:57-66.
7. Tomalka AG, Stopford CM, Lee PC, Rietsch A. 2012. A translocatorspecific export signal establishes the translocator-effector secretion hierarchy that is important for type III secretion system function. Mol. Microbiol. 86:1464-1481.
8. Parsot C, Hamiaux C, Page AL. 2003. The various and varying roles of specific chaperones in type III secretion systems. Curr. Opin. Microbiol. 6:7-14.
9. Büttner CR, Sorg I, Cornelis GR, Heinz DW, Niemann HH. 2008. Structure of the Yersinia enterocolitica type III secretion translocator chaperone SycD. J. Mol. Biol. 375:997-1012.
10. Lunelli M, Lokareddy RK, Zychlinsky A, Kolbe M. 2009. IpaB-IpgC interaction defines binding motif for type III secretion translocator. Proc. Natl. Acad. Sci. U. S. A. 106:9661-9666.
11. Job V, Mattei PJ, Lemaire D, Attree I, Dessen A. 2010. Structural basis of chaperone recognition of type III secretion system minor translocator proteins. J. Biol. Chem. 285:23224-23232.
12. Singh SK, Boyle AL, Main ER. 2013. LcrH, a class II chaperone from the type three secretion system, has a highly flexible native structure. J. Biol. Chem. 288:4048-4055.
13. Lokareddy RK, Lunelli M, Eilers B, Wolter V, Kolbe M. 2010. Combination of two separate binding domains defines stoichiometry between type III secretion system chaperone IpgC and translocator protein IpaB. J. Biol. Chem. 285:39965-39975.
14. Barta ML, Zhang L, Picking WL, Geisbrecht BV. 2010. Evidence for alternative quaternary structure in a bacterial type III secretion system chaperone. BMC Struct. Biol. 10:21. doi:10.1186/1472-6807-10-21.
15. Birket SE, Harrington AT, Espina M, Smith ND, Terry CM, Darboe N, Markham AP, Middaugh CR, Picking WL, Picking WD. 2007. Preparation and characterization of translocator/chaperone complexes and their component proteins from Shigella flexneri. Biochemistry 46:8128- 8137.
16. Lerner CG, Inouye M. 1990. Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability. Nucleic Acids Res. 18:4631.
17. Cisz .M. Lee PC, Rietsch A. 2008. ExoS controls the cell contact-mediated switch to effector secretion in Pseudomonas aeruginosa. J. Bacteriol. 190: 2726-2738.
18. Miller JH. 1992. A short course in bacterial genetics: a laboratory manual and handbook for Escherichia coli and related bacteria. Cold Spring Harbor Laboratory Press, Plainview, NY.
19. Dove SL, Hochschild A. 2004. A bacterial two-hybrid system based on transcription activation. Methods Mol. Biol. 261:231-246.
20. Vallet-Gely I, Donovan KE, Fang R, Joung JK, Dove SL. 2005. Repression of phase-variable cup gene expression by H-NS-like proteins in Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. U. S. A. 102:11082-11087.
21. Wolfgang MC, Lee VT, Gilmore ME, Lory S. 2003. Coordinate regulation of bacterial virulence genes by a novel adenylate cyclase-dependent signaling pathway. Dev. Cell 4:253-263.
22. Edqvist PJ, Broms JE, Betts HJ, Forsberg A, Pallen MJ, Francis MS. 2006. Tetratricopeptide repeats in the type III secretion chaperone, LcrH: their role in substrate binding and secretion. Mol. Microbiol. 59:31-44.
23. Castang S, Dove SL. 2010. High-order oligomerization is required for the function of the H-NS family member MvaT in Pseudomonas aeruginosa. Mol. Microbiol. 78:916-931.
24. Lee PC, Stopford CM, Svenson AG, Rietsch A. 2010. Control of effector export by the Pseudomonas aeruginosa type III secretion proteins PcrG and PcrV. Mol. Microbiol. 75:924-941.