Reversible unfolding of sheep liver tetrameric serine hydroxymethyltransferase

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1384, Issue 1, 1998, Pages 141-152

  Venkatesha, B ^a   Udgaonkar, Jayant B ^a   Rao, N Appaji ^a   Savithri, H S ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Oligomeric protein; PLP dependent enzyme; Reversible ullfolding; SHMT; Urea denaturation

Indexed keywords

GLYCINE HYDROXYMETHYLTRANSFERASE; PYRIDOXAL 5 PHOSPHATE; UREA;

ANIMAL TISSUE; ARTICLE; CIRCULAR DICHROISM; DENATURATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STRUCTURE; GEL PERMEATION CHROMATOGRAPHY; LIVER; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SHEEP;

ANIMALS; CIRCULAR DICHROISM; GLYCINE HYDROXYMETHYLTRANSFERASE; LIVER; PROTEIN FOLDING; SHEEP;

ANIMALIA; OVIS ARIES;

EID: 0032560031     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00013-2     Document Type: Article

References (47)

1. Jaenicke R. Folding and association of proteins. Prog. Biophys. Mol. Biol. 49:1987;117-237.
2. Seckler R., Jaenicke R. Protein folding and protein refolding. FASEB J. 6:1992;2545-2552.
3. West S.M., Price N.C. The unfolding and refolding of cytoplasmic asparate aminotransferase from pig heart. Biochem. J. 261:1989;189-196.
4. West S.M., Price N.C. The unfolding and attempted refolding of mitochondrial aspartate aminotransferase from pig heart. Biochem. J. 265:1990;45-50.
5. Herold M., Kirschner K. Reversible dissociation and unfolding of aspartate aminotransferase from E. coli; characterization of a monomeric intermediate. Biochemistry. 29:1990;1907-1913.
6. Herold M., Leistler B. Unfolding of truncated and wild type asparate aminotransferase studied by size exclusion chromatography. J. Chromatogr. 539:1991;383-391.
7. Herold M., Leistler B., Hage A., Luger K., Kirschner K. Autonomous folding and coenzyme binding of the excised pyridoxal 5′-phosphate binding domain of aspartate aminotransferase from Escherichia coli. Biochemistry. 30:1991;3612-3620.
8. Herold M., Leistler B. Coenzyme binding of a folding intermediate of asparate aminotransferase detected by HPLC fluorescence measurements. FEBS Lett. 308:1992;26-29.
9. Reyes A.M., Iriarte A., Carrion M.M. Refolding of the precursor and the mature forms of mitochondrial asparate aminotransferase after guanidine hydrochloride denaturation. J. Biol. Chem. 268:1993;22281-22291.
10. Artigues A., Iriarte A., Carrion M.M. Acid induced reversible unfolding of mitochondrial aspartate aminotransferase. J. Biol. Chem. 269:1994;21990-21999.
11. Artigues A., Iriarte A., Carrion M.M. Refolding intermediates of acid unfolded mitochondrial aspartate aminotransferase bind to hsp70. J. Biol. Chem. 272:1997;16852-16861.
12. Matthews C.R., Crisanti M.M. Urea induced unfolding of the α-subunit of tryptophan synthase; evidence for a multistate process. Biochemistry. 20:1981;784-792.
13. Blond S., Goldberg M.E. Kinetics and importance of the dimerization step in the folding pathway of beta 2 subunit of Escherichia coli tryptophan synthase. J. Mol. Biol. 182:1985;597-606.
14. Blond S., Goldberg M.E. Kinetic characterization of early intermediates in the folding of E. coli tryptophan-synthase beta 2 subunit. Proteins. 1:1986;247-255.
15. Goldberg M.E., Semisotnov G.V., Friguet B., Kuwajiama K., Ptitsyn O.B., Sugai S. An early immunoreactive folding intermediate of tryptophan synthase beta 2 subunit is a molten globule. FEBS Lett. 263:1990;51-56.
16. Goldberg M.E. Investigating protein conformation, dynamics and folding with monoclonal antibodies. Trends Biochem. Sci. 16(10):1991;358-362.
17. Kanzaki H., McPhie P., Miles E.W. Effect of single amino acid substitutions at positions 49 and 60 on the thermal unfolding of the tryptophan synthase α subunit from Salmonella typhimurium. Arch. Biochem. Biophys. 284:1991;174-180.
18. Chaffotte A.F., Cadieux C., Guillou Y., Goldberg M.E. A possible initial folding intermediate; the C-terminal proteolytic domain of tryptophan synthase beta chains folds in less than 4 milliseconds into a condensed state with non-native-like secondary structure. Biochemistry. 31:1992;4303-4308.
19. Ahmed S.A., McPhie P., Miles E.W. A thermally induced reversible conformation transition of the tryptophan synthase β2 subunit probed by the spectroscopic properties of pyridoxal phosphate and by enzymatic activity. J. Biol. Chem. 271:1996;8612-8617.
20. Ogasahara K., Matsushita E., Yutani K. Further examination of the intermediate state in the denaturation of the tryptophan synthase α subunit; evidence that the equilibrium denaturation intermediate is a molten globule. J. Mol. Biol. 234:1993;1197-1206.
21. Choi S.-G., O'Donnell S.E., Sarken K.D., Hardman J.K. Tryptophan containing α-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties. J. Biol. Chem. 270:1995;17712-17715.
22. Guijarro J.I., Jackson M., Chaffotte A.F., Delepierre M., Mantsch H.H., Goldberg M.E. Protein folding intermediates with rapidly exchangeable amide protons contain authentic hydrogen-bonded secondary structures. Biochemistry. 34:1995;2998-3008.
23. Planchenault T., Navon A., Schulze A.J., Goldberg M.E. Transient non-native interactions in early folding intermediates do not influence the folding kinetics of Escherichia coli tryptophan synthase beta 2 subunits. Eur. J. Biochem. 240:1996;615-621.
24. Chaffotte A.F., Guijarro J.I., Guillou Y., Delepierre M., Goldberg M.E. The 'pre-molten globule' a new intermediate in protein folding. J. Protein Chem. 16:1997;433-439.
25. 2 complex. Stabilization by PLP aldimine intermediates. J. Biol. Chem. 270:1995;7944-7949.
26. Schirch L. Serine hydroxymethyltransferase. Adv. Enzymol. 53:1982;83-112.
27. Appaji Rao N., Ramesh K.S., Manohar R., Rao D.N., Vijayalakshmi D., Baskaran N. Serine hydroxymethyltransferase: active site interactions and role in cell proliferation. J. Sci. Ind. Res. 46:1987;248-260.
28. Usha R., Savithri H.S., Rao N.A. The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferase. Biochim. Biophys. Acta. 1204:1994;75-83.
29. Jagath-Reddy J., Ganesan K., Savithri H.S., Datta A., Appaji Rao N. cDNA cloning, overexpression in E. coli, purification and characterization of sheep liver cytosolic serine hydroxymethyltransferase. Eur. J. Biochem. 230:1995;533-537.
30. Grishin N.V., Phillips M.A., Goldsmith E.J. Modeling of the spatial structure of eukaryotic ornithine decarboxylases. Protein Sci. 4:1995;1291-1304.
31. Alexander F.W., Sandmeier E., Mehta P.K., Christen P. Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes; regio-specific α, β and γ families. Biochem. J. 219:1994;953-960.
32. Brahatheeswaran B., Prakash V., Savithri H.S., Rao N.A. Interaction of sheep liver apo-serine hydroxymethyltransferase with pyridoxal-5′-phosphate; a physicochemical, kinetic and thermodynamic study. Arch. Biochem. Biophys. 330:1996;363-372.
33. Jagath J.R., Sharma B., Bhaskar B., Datta A., Rao N.A., Savithri H.S. Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase. Eur. J. Biochem. 247:1997;372-379.
34. Cai K., Schirch D., Schirch V. The affinity of pyridoxal-5′-phosphate for folding intermediates of E. coli serine hydroxymethyltransferase. J. Biol. Chem. 270:1995;19294-19299.
35. Hatefi Y., Talbert P.T., Osborn M.J., Huennekens F.M. Tetrahydrofolic acid-5,6,7,8-tetrahydropteroylglutamic acid. Biochem. Prep. 7:1959;89-92.
36. Baskaran N., Prakash V., Appu Rao A.G., Radhakrishnan A.N., Savithri H.S., Appaji Rao N. Mechanism of interaction of O-amino-D-serine with sheep liver serine hydroxymethyltransferase. Biochemistry. 28:1989;9607-9612.
37. Schirch D., Fratte S.D., Iuresia S., Angelaccio S., Contestabile R., Bossa F., Schirch V. Function of the active site lysine in Escherichia coli serine hydroxymethyltransferase. J. Biol. Chem. 268:1993;23132-23138.
38. Lowry O.H., Rosenbrough N.J., Farr A.L., Randall R.J. Protein measurement with the Folin-phenol reagent. J. Biol. Chem. 193:1951;265-275.
39. Manohar R., Ramesh K.S., Appaji Rao N. Purification, physicochemical regulatory properties of serine hydroxymethyltransferase from sheep liver. J. Biosci. 4:1982;31-50.
40. J.E. Churchich, Coenzymes and Cofactors, in: D. Dolphin, R. Poulson, O. Avramovic (Ed.), Vitamin B6, Pyridoxal Phosphate, Chemical, Biochemical, and Medical Aspects, Vol. 1, Part A., Wiley, New York, 1986, pp. 545-567.
41. R. Jaenicke, R. Rudolph, Folding and association of oligomeric proteins, in: R. Jaenicke (Ed.), Protein Folding, North-Holland, Amsterdam, 1980, pp. 525-548.
42. M.G. Rossman, A. Liljas, C.-I. Branden, L.J. Banaszak, The Enzymes, in: P.D. Boyer (Ed.), 3rd edn., Vol. XI, Academic Press, New York, 1975, pp. 61-102.
43. Lovell S.J., Winzor D.J. Effects of phosphates on the dissociation and enzymatic stability of rabbit muscle lactate dehydrogenase. Biochemistry. 13:1974;3527-3531.
44. Vallee R.B., Williams R.C. The two step reversible denaturation of lactate dehydrogenase at low pH. Biochemistry. 14:1975;2574-2580.
45. O.B. Ptitsyn, The Molten Globule State, Protein Folding, in: T.E. Creighton (Ed.), Freeman, New York, 1992.
46. Cai K., Schirch V. Structural studies on folding intermediates of serine hydroxymethyltransferase using single tryptophan mutants. J. Biol. Chem. 271:1996;2987-2994.
47. Cai K., Schirch V. Structural studies on folding intermediates of serine hydroxymethyltransferase using fluorescence resonance energy transfer. J. Biol. Chem. 271:1996;27311-27320.