Cooperative effects of potassium, magnesium, and magnesium-ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL

Protein Science

Volumn 8, Issue 10, 1999, Pages 2166-2176

  Clark, A Clay ^a,b   Karon, Brad S ^a   Frieden, Carl ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

Conformational changes; Ligand binding; Protein folding

Indexed keywords

ADENOSINE DIPHOSPHATE; CHAPERONIN; DIHYDROFOLATE REDUCTASE; MAGNESIUM; POTASSIUM;

ARTICLE; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; ENZYME BINDING; ENZYME CONFORMATION; ENZYME RELEASE; LIGAND BINDING; MATHEMATICAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0032885222     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.10.2166     Document Type: Article

References (36)

1. Ahrweiler PM, Frieden C. 1991. Effects of point mutations in a hinge region on the stability, folding, and enzymatic activity of Escherichia coli dihydrofolate reductase. Biochemistry 30:7801-7809.
2. Azem A, Diamant S, Goloubinoff P. 1994. Effect of divalent cations on the molecular structure of the GroEL oligomer. Biochemistry 33:6671-6675.
3. Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB. 1994. The crystal structure of the bacterial chaperonin GroEL at 2.8 D. Nature 371:578-586.
4. Cayley PJ, Dunn SMJ, King RW. 1981. Kinetics of substrate, coenzyme, and inhibitor binding to Escherichia coli dihydrofolate reductase. Biochemistry 20:874-879.
5. Clark AC, Frieden C. 1999a. Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures. J Mol Biol 285:1765-1776.
6. Clark AC, Frieden C. 1999b. The chaperonin GroEL binds late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases. J Mol Biol 285:1777-1788.
7. Clark AC, Frieden C. 1997. GroEL-mediated folding of structurally homologous dihydrofolate reductases. J Mol Biol 268:512-525.
8. Clark AC, Hugo E, Frieden C. 1996. Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL. Biochemistry 35:5893-5901.
9. Clark AC, Ramanathan R, Frieden C. 1998. Purification of GroEL with low fluorescence background. Methods Enzymol 290:100-118.
10. 14. Biochemistry 34:213-277.
11. Dunn SMJ, Batchelor JG, King RW. 1978. Kinetics of ligand binding to dihydrofolate reductase: Binary complex formation with NADPH and coenzyme analogues. Biochemistry 17:2356-2364.
12. Fenton WA, Horwich AL. 1997. GroEL-mediated protein folding. Protein Sci 6:743-760.
13. Fisher MT. 1992. Promotion of in vitro renaturation of dodecameric glutamine synthetase form Escherichia coli in the presence of GroEL (chaperonin-60) and ATP. Biochemistry 31:3955-3963.
14. Frieden C. 1990. Refolding of Escherichia coli dihydrofolate reductase: Sequential formation of substrate binding sites. Proc Natl Acad Sci USA 87:4413-4416.
15. Frieden C, Clark AC. 1997. Protein folding: How the mechanism of GroEL action is defined by kinetics. Proc Natl Acad Sci USA 94:5535-5538.
16. Gibbons DL, Horowitz PM. 1996. Ligand-induced conformational changes in the apical domain of the chaperonin GroEL. J Biol Chem 271:238-243.
17. Hayer-Hartl MK, Weber F, Hartl FU. 1996. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J 15:6111-6121.
18. Hendrix RW. 1979. Purification and properties of groE, a host protein involved in bacteriophage assembly. J Mol Biol 129:375-392.
19. Hill AV. 1910. The possible effect of the aggregation of the molecules of hemoglobin on its dissociation curves. J Physiol Soc (Proceedings) 40:iv-vii.
20. Hoeltzli SD, Frieden C. 1994. 19F NMR spectroscopy of [6-19F]tryptophanlabeled Escherichia coli dihydrofolate reductase: Equilibrium folding and ligand binding studies. Biochemistry 33:5502-5509.
21. Jackson GS, Staniforth RA, Halsall DJ, Atkinson T, Holbrook JJ, Clarke AR, Burston SG. 1993. Binding and hydrolysis of nucleotides in the chaperonin cycle: Implications for the mechanism of assisted protein folding. Biochemistry 32:2554-2563.
22. Lin Z, Eisenstein E. 1996. Nucleotide binding-promoted conformational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL. Proc Natl Acad Sci USA 93:1977-1981.
23. Llorca O, Perez-Perez J, Carrascosa JL, Galan A, Muga A, Valpuesta JM. 1997. Effects of inter-ring communication in GroEL structural and functional asymmetry. J Biol Chem 272:32925-32932.
24. Pace CN, Shirley BA, Thompson JA. 1989. Measuring the conformational stability of a protein. In: Creighton T, ed. Protein structure and function, a practical approach. New York: IRL Press. pp 311-329.
25. Penner MH, Frieden C. 1987. Kinetic analysis of the mechanism of Escherichia coli dihydrofolate reductase. J Biol Chem 202:15908-15914.
26. Rye HS, Burston SG, Fenton WA, Beechem JM, Xu Z, Sigler PB, Horwich AL. 1997. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 388:792-798.
27. Sigler PB, Xu Z, Rye HS, Burston SG, Fenton WA, Horwich AL. 1998. Structure and function in GroEL-mediated protein folding. Anna Rev Biochem 67:581-608.
28. Todd MJ, Viitanen PV, Lorimer GH. 1993. Hydrolysis of adenosine 5′-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion. Biochemistry 2:8560-8567.
29. Todd MJ, Viitanen PV, Lorimer GH. 1994. Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding. Science 265:659-666.
30. Touchette NA, Perry KM, Matthews CR. 1986. Folding of dihydrofolate reductase from Escherichia coli. Biochemistry 25:5445-5452.
31. + dependent. Biochemistry 29:5665-5611.
32. Weissman JS, Hohl CM, Kovalenko O, Kashi Y, Chen S, Braig K, Saihil HR, Fenton WA, Horwich AL. 1995. Mechanism of GroEL action: Productive release of polypeptide form a sequestered position under GroES. Cell 83:577-687.
33. Weissman JS, Rye HS, Fenton WA, Beechem JM, Horwich AL. 1996. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84:481-490.
34. Yifrach O, Horovitz A. 1995. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry 34:5303-5308.
35. Yifrach O, Horovitz A. 1996. Allosteric control by ATP of non-folded protein binding to GroEL. J Mol Biol 255:356-361.
36. Yifrach O, Horovitz A. 1998. Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL. Biochemistry 37:7083-7088.