The influence of C-terminal extension on the structure of the 'J- domain' in E. coli DnaJ

Protein Science

Volumn 8, Issue 1, 1999, Pages 203-214

  Huang, Kai ^a   Flanagan, John M ^b   Prestegard, James H ^c  

^a YALE UNIVERSITY   (United States)

^b BROOKHAVEN NATIONAL LABORATORY   (United States)

^c UNIVERSITY OF GEORGIA   (United States)

Author keywords

ATPase stimulatory activity; DnaJ; Heat shock protein; Molecular chaperone; NMR structure

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CARBON 13; CHAPERONE; HEAT SHOCK PROTEIN; HELIX LOOP HELIX PROTEIN; NITROGEN 15;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE;

EID: 0032947385     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.1.203     Document Type: Article

References (54)

1. β resonance in larger proteins. J Magn Reson 95:636-641.
2. Auger I, Roudier J. 1997. A function for the QKRAA amino acid motif: Mediating binding of DnaJ to DnaK: Implications for the association of rheumatoid arthritis with HLA-DR4. J Clin Invest 99:1818-1822.
3. Bai Y, Milne JS, Mayne L, Englander SW. 1993. Primary structure effects on peptide group hydrogen exchange. Proteins Struct Funct Genet 17:75-86.
4. Banecki B, Zylicz M. 1996. Real time kinetics of the DnaK-DnaJ-GrpE molecular chaperone machine action. J Biol Chem 271:6137-6143.
5. + gene: A gene that encodes a heat shock protein. J Biol Chem 261:1782-1785.
6. 13C-labeled proteins. J Magn Reson 87:620-627.
7. Bork P, Sander C, Valencia A, Bukau B. 1992. A module of the DnaJ heat shock proteins found in malaria parasites. TIBS 17:129.
8. 15N "random coil" chemical shifts. J Am Chem Soc 116:8466-8469.
9. Brunger AT. 1992. X-PLOR version 3.1: A system for X-ray crystallography and NMR. New Haven, Connecticut USA: Yale University.
10. 13C separated rotating frame Overhauser spectroscopy. J Biomol NMR 1:13-22.
11. Connelly GP, Bai Y, Jeng MF, Englander SW. 1993. Isotope effects in peptide group hydrogen exchange. Proteins Struct Funct Genet 17:87-92.
12. Ferrin TE, Huang CC, Jarvis LE, Langridge R. 1988. The MIDAS display system. J Mol Graphics 6:13-27.
13. Gemmecker G, Jahnke W, Kessler H. 1993. Measurement of fast proton exchange rates in isotopically labeled compounds. J Am Chem Soc 115:11620-11621.
14. Greene MK, Maskos K, Landry SJ. 1998. Role of the J-domain in the cooperation of Hsp 40 with Hsp 70. Proc Natl Acad Sci USA 95:6108-6113.
15. 2O in protein NMR. Application to sensitivity enhancement and NOE measurement. J Am Chem Soc 115:12593-12594.
16. Grzesiek S, Vuister GW, Bax A. 1993. A simple and sensitive experiment for measurement of Jcc couplings between backbone carbonyl and methyl carbons in isotopically enriched proteins. J Biomol NMR 3:487-493.
17. Hendrick JP, Langer T, Davis TA, Hartl FU, Wiedmann M. 1993. Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc Natl Acad Sci USA 90:10216-10220.
18. 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ (1-78). Biochemistry 34:5587-5596.
19. 13C-labeled protein. J Magn Reson 86:204-209.
20. Karzai AW, McMacken R. 1996. A bipartite signaling mechanism involved in DnaJ-medialed activation of the Escherichia coli DnaK protein. J Biol Chem 271:11236-11246.
21. Kay LE, Keifer P, Saarinen T. 1992. Pure absorption enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665.
22. 2O samples of proteins. J Magni Reson 101 B:333-337.
23. Kudlicki W, Odorn OW, Kramer G, Hardesty B. 1996. Binding of an N-terminal rhodanese peptide to DnaJ and to ribosomes. J Biol Chem 271:31160-31165.
24. Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU. 1992. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356:683-689.
25. Laskowski RA, Rullmann JAC, MacArthur MW, Kaptein R, Thornton JM. 1996. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8:477-486.
26. Liberek K, Marszalek J, Ang D, Georgopoulos C. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci USA 88:2874-2878.
27. Muhandiram DR, Kay LE. 1994. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J Magn Reson 103 B:203-216.
28. 15N spectroscopy. J Magn Reson 87:488-501.
29. Ohki M, Tamura F, Nishimura S, Uchida H. 1986. Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product. J Biol Chem 261:1778-1781.
30. Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wüthrich K. 1996. NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J Mol Biol 260:236-250.
31. Piotto M, Saudek V. Sklenar V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2:661-665.
32. Qian YQ, Patel D, Hartl FU, McColl DJ. 1996. Nuclear magnetic resonance solution structure of the human hsp40 (HDJ-1) J-domain. J Mol Biol 260:224-235.
33. Rice LM, Brunger AT. 1994. Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement. Proteins Struct Funct Genet 19:277-290.
34. Richards FM, Kundrot CE. 1988. Identification of structural motifs from protein coordinate data: Secondary structure and first-level supersecondary structure. Proteins Struct Funct Genet 3:71-84.
35. Saito H, Uchida H. 1977. Initiation of the DNA replication of bacteriophage λ in E. coli K12. J Mol Biol 113:1-25.
36. Stein EG, Rice LM, Brunger AT. 1997. Torsion angle molecular dynamics as a new efficient tool for NMR structure calculation. J Magn Reson 124:154-164.
37. Straus D, Walter WA, Gross CA. 1988. Escherichia coli heat shock gene mutants are defective in proteolysis. Genes & Dev 2:1851-1858.
38. 32. Genes & Dev 4:2202-2209.
39. Sunshine M, Feiss M, Stuart J, Yochem J. 1977. A new host gene (groPC) necessary for λ DNA replication. Mol Gen Genet 151:27-34.
40. Szabo A, Korszun R, Hartl FU, Flanagan J. 1996. A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J 15:408-417.
41. Szyperski T, Pellecchia M, Wall D, Georgopoulos C, Wüthrich K. 1994. NMR structure determination of the Escherichia coli DnaJ molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain. Proc Natl Acad Sci USA 91:11343-11347.
42. Tsai J, Douglas MG. 1996. A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. J Biol Chem 271:9347-9354.
43. 13C decoupling. J Magn Reson 98:428-435.
44. 15N-enriched proteins. J Am Chem Soc 115:7772-7777.
45. 13C. J Am Chem Soc 115:5334-5335.
46. 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication. J Biol Chem 269:5446-5451.
47. Wall D, Zylicz M, Georgopoulos C. 1995. The conserved G/F Motif of the DnaJ chaperone is necessary for the activation of the DnaK chaperone. J Biol Chem 270:2139-2144.
48. Wickner S, Hoskins J, McKenney K. 1991. Monomerization of repA dimers by heat shock proteins activates binding to DNA replication origin. Proc Natl Acad Sci USA 88:7903-7907.
49. 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6:135-140.
50. 13C chemical-shift data. J Biomol NMR 4:171-180.
51. Wishart DS, Sykes BD, Richards FM. 1992. The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647-1651.
52. Wüthrich K. 1986. NMR of proteins and nucleic acids. New York: Wiley.
53. Wüthrich K, Billeter M, Braun W. 1983. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J Mol Biol 169:949-961.
54. 13C-labeled proteins via scalar couplings. J Am Chem Soc 115:11054-11055.