Analysis of the function of mycobacterial DnaJ proteins by overexpression and microarray profiling

Tuberculosis

Volumn 84, Issue 3-4, 2004, Pages 180-187

  Stewart, Graham R ^a   Robertson, Brian D ^a   Young, Douglas B ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

Chaperone; DnaA; Heat shock protein; Mycobacterium tuberculosis

Indexed keywords

DEOXYRIBONUCLEOPROTEIN; DNA A; PEPTIDE; PROTEIN DNAJ;

ARTICLE; BACTERIAL GENE; BACTERIAL INFECTION; CHROMOSOME REPLICATION; DNA FLANKING REGION; DNA MICROARRAY; ESSENTIAL GENE; GENE CONTROL; GENE DELETION; GENE EXPRESSION; GENE FUNCTION; GENETIC TRANSCRIPTION; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION;

AMINO ACID SEQUENCE; GENE EXPRESSION REGULATION, BACTERIAL; GENES, BACTERIAL; GENETIC VECTORS; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM BOVIS; MYCOBACTERIUM TUBERCULOSIS; OLIGONUCLEOTIDE ARRAY SEQUENCE ANALYSIS; SEQUENCE ALIGNMENT; TRANSCRIPTION, GENETIC;

EID: 3042708984     PISSN: 14729792     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tube.2003.12.009     Document Type: Article

References (47)

1. Hartl F.U., Hayer-Hartl M. Molecular chaperones in the cytosol. from nascent chain to folded protein Science. 295(5561):2002;1852-1858
2. Hartl F.U. Molecular chaperones in cellular protein folding. Nature. 381(6583):1996;571-579
3. Lindquist S., Craig E.A. The heat-shock proteins. Annu Rev Genet. 22:1988;631-677
4. Buchmeier N.A., Heffron F. Induction of Salmonella stress proteins upon infection of macrophages. Science. 248(4956):1990;730-732
5. Lee B.Y., Horwitz M.A. Identification of macrophage and stress-induced proteins of Mycobacterium tuberculosis. J Clin Invest. 96(1):1995;245-249
6. Monahan I.M., Betts J., Banerjee D.K., Butcher P.D. Differential expression of mycobacterial proteins following phagocytosis by macrophages. Microbiology. 147(Part 2):2001;459-471
7. Becker T., Hartl F.U., Wieland F. CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. J Cell Biol. 158(7):2002;1277- 1285
8. Wang Y., Kelly C.G., Karttunen J.T., et al. CD40 is a cellular receptor mediating mycobacterial heat shock protein 70 stimulation of CC-chemokines. Immunity. 15(6):2001;971-983
9. Basu S., Binder R.J., Ramalingam T., Srivastava P.K. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity. 14(3):2001;303-313
10. Asea A., Rehli M., Kabingu E., et al. Novel signal transduction pathway utilized by extracellular HSP70. role of toll-like receptor (TLR)2 and TLR4 J Biol Chem. 277(17):2002;15028-15034
11. Habich C., Baumgart K., Kolb H., Burkart V. The receptor for heat shock protein 60 on macrophages is saturable, specific, and distinct from receptors for other heat shock proteins. J Immunol. 168(2):2002;569-576
12. Asea A., Kraeft S.K., Kurt-Jones E.A., et al. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med. 6(4):2000;435-442
13. Lehner T., Bergmeier L.A., Wang Y., et al. Heat shock proteins generate beta-chemokines which function as innate adjuvants enhancing adaptive immunity. Eur J Immunol. 30(2):2000;594-603
14. Castellino F., Boucher P.E., Eichelberg K., et al. Receptor-mediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways. J Exp Med. 191(11):2000;1957-1964
15. Huang Q., Richmond J.F., Suzue K., Eisen H.N., Young R.A. In vivo cytotoxic T lymphocyte elicitation by mycobacterial heat shock protein 70 fusion proteins maps to a discrete domain and is CD4(+) T cell independent. J Exp Med. 191(2):2000;403-408
16. Suto R., Srivastava P.K. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science. 269(5230):1995;1585-1588
17. Srivastava P.K., Menoret A., Basu S., Binder R.J., McQuade K.L. Heat shock proteins come of age. primitive functions acquire new roles in an adaptive world Immunity. 8(6):1998;657-665
18. Stewart G.R., Snewin V.A., Walzl G., et al. Overexpression of heat-shock proteins reduces survival of Mycobacterium tuberculosis in the chronic phase of infection. Nat Med. 7(6):2001;732-737
19. Game J., Multhaup G., Tomoyasu T., et al. A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 15(3):1996;607-617
20. Schroder H., Langer T., Hartl F.U., Bukau B. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12(11):1993;4137-4144
21. Szabo A., Langer T., Schroder H., Flanagan J., Bukau B., Hartl F.U. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc Natl Acad Sci USA. 91(22):1994;10345-10349
22. Wawrzynow A., Banecki B., Wall D., Liberek K., Georgopoulos C., Zylicz M. ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates. J Biol Chem. 270(33):1995;19307-19311
23. Laufen T., Mayer M.P., Beisel C., et al. Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones. Proc Natl Acad Sci USA. 96(10):1999;5452-5457
24. Karzai A.W., McMacken R. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J Biol Chem. 271(19):1996;11236-11246
25. Silberg J.J., Hoff K.G., Vickery L.E. The Hsc66-Hsc20 chaperone system in Escherichia coli. chaperone activity and interactions with the DnaK-DnaJ-GrpE system J Bacteriol. 180(24):1998;6617-6624
26. Yoshimune K., Yoshimura T., Nakayama T., Nishino T., Esaki N. Hsc62, Hsc56, and GrpE, the third Hsp70 chaperone system of Escherichia coli. Biochem Biophys Res Commun. 293(5):2002;1389-1395
27. Cole S.T., Brosch R., Parkhill J., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 393(6685):1998;537-544
28. Stewart G.R., Wernisch L., Stabler R., et al. Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays. Microbiology. 148(Part 10):2002;3129-3138
29. Kenney T.J., Churchward G. Genetic analysis of the Mycobacterium smegmatis rpsL promoter. J Bacteriol. 178(12):1996;3564-3571
30. Wards B.J., Collins D.M. Electroporation at elevated temperatures substantially improves transformation efficiency of slow-growing mycobacteria. FEMS Microbiol Lett. 145(1):1996;101-105
31. Wilson M., DeRisi J., Kristensen H.H., et al. Exploring drug-induced alterations in gene expression in Mycobacterium tuberculosis by microarray hybridization. Proc Natl Acad Sci USA. 96(22):1999;12833-12838
32. Wilson M, Voskuil M, Schnappinger D, Schoolnik GK, editors. Functional genomics of Mycobacterium tuberculosis using DNA microarrays. In: Parish T., Stoker N.G. (Ed.) Methods in Molecular Medicine, Mycobacterium tuberculosis Protocols, Vol. 54. Clifton, UK: Humanae Press, 2001.
33. Tusher V.G., Tibshirani R., Chu G. Significance analysis of microarrays applied to the ionizing radiation response. Proc Natl Acad Sci USA. 98(9):2001;5116-5121
34. Packschies L., Theyssen H., Buchberger A., Bukau B., Goody R.S., Reinstein J. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry. 36(12):1997;3417-3422
35. Liberek K., Marszalek J., Ang D., Georgopoulos C., Zylicz M. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci USA. 88(7):1991;2874-2878
36. Bucca G., Brassington A.M., Schonfeld H.J., Smith C.P. The HspR regulon of Streptomyces coelicolor. a role for the DnaK chaperone as a transcriptional co-repressor Mol Microbiol. 38(5):2000;1093-1103
37. Liberek K., Wall D., Georgopoulos C. The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator. Proc Natl Acad Sci USA. 92(14):1995;6224-6228
38. Zylicz M., Ang D., Liberek K., Georgopoulos C. Initiation of lambda DNA replication with purified host - and bacteriophage - encoded proteins. the role of the DnaK, DnaJ and GrpE heat shock proteins EMBO J. 8(5):1989;1601-1608
39. Alfano C., McMacken R. Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage lambda DNA replication. J Biol Chem. 264(18):1989;10709-10718
40. Wickner S., Hoskins J., McKenney K. Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin. Proc Natl Acad Sci USA. 88(18):1991;7903-7907
41. Konieczny I., Liberek K. Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein. J Biol Chem. 277(21):2002;18483-18488
42. Ezaki B., Ogura T., Mori H., Niki H., Hiraga S. Involvement of DnaK protein in mini-F plasmid replication. temperature-sensitive seg mutations are located in the dnaK gene Mol Gen Genet. 218(2):1989;183-189
43. Hwang D.S., Crooke E., Kornberg A. Aggregated dnaA protein is dissociated and activated for DNA replication by phospholipase or DnaK protein. J Biol Chem. 265(31):1990;19244-19248
44. Lee Y.S., Hwang D.S. Occlusion of RNA polymerase by oligomerization of DnaA protein over the dnaA promoter of Escherichia coli. J Biol Chem. 272(1):1997;83-88
45. Wickner S., Hoskins J., McKenney K. Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA. Nature. 350(6314):1991;165- 167
46. Fisher M.A., Plikaytis B.B., Shinnick T.M. Microarray analysis of the Mycobacterium tuberculosis transcriptional response to the acidic conditions found in phagosomes. J Bacteriol. 184(14):2002;4025-4032
47. Betts J.C., Lukey P.T., Robb L.C., McAdam R.A., Duncan K. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol Microbiol. 43(3):2002;717-731