Site-directed mutagenesis of proline 204 in the 'hinge' region of yeast phosphoglycerate kinase

European Journal of Biochemistry

Volumn 259, Issue 3, 1999, Pages 939-946

  McHarg, Jane ^b   Kelly, Sharon M ^b   Price, Nicholas C ^b   Cooper, Alan ^b   Littlechild, Jennifer A ^a  

^a UNIVERSITY OF EXETER   (United Kingdom)

^b NONE

Author keywords

cis proline; Microdomains; Phosphoglycerate kinase; Site directed mutagenesis; Stability

Indexed keywords

PHOSPHOGLYCERATE KINASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME STABILITY; GLUCONEOGENESIS; GLYCOLYSIS; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; YEAST;

EID: 0001060193     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00133.x     Document Type: Article

References (31)

1. 1. Hess, D., Kruger, K., Knappik, A., Palm, P. & Hensel, R. (1995) Dimeric 3-phosphoglycerate kinases from hyperthermophilic archaea - Cloning, sequencing and expression of the 3-phosphoglycerate kinase gene of Pyrococcus woesei in E. coli and characterisation of the protein - Structural and functional comparison wilh the 3-phosphoglycerate kinase of Methanothermus fervidus. Eur. J. Biochem. 233, 227-237.
2. 2. Jones, C.E., Fleming, T.M., Cowan, D.A., Littlechild, J.A. & Piper, P.W. (1995) The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeon Sulpholobus solfataricus overlap by 8 bp: isolation, sequencing of the genes and expression in Escherichia coli. Eur. J. Blochem. 223, 800-808.
3. 3. Harlos, K., Vas, M. & Blake, C.F. (1992) Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate. Proteins 12, 133-144.
4. 4. Davies, G.J., Gamblin, S.J., Littlechild, J.A., Dauter, Z., Wilson, K.S. & Watson, H.C. (1994) Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65Å. Acta Crystallogr. D50, 202-209.
5. 5. Watson, H.C. & Littlechild, J.A. (1990) Isoenzymes of phosphoglycerate kinase: Evolutionary conservation of the structure of this glycolytic enzyme. Biochem. Soc. Trans. 18, 187-190.
6. 6. Banks, R.D., Blake, C.C.F., Evans, P.R., Haser, R., Rice, D.W., Hardy, G.W., Merret, M. & Phillips, A.W. (1979) Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme. Nature 279, 773-777.
7. 7. Watson, H.C., Walker, N.P.C., Shaw, P.J., Bryant, T.N., Wendell, P.L., Fothergill, L.A., Perkins, R.E., Conroy, S.C., Dobson, M.J., Tuite, M.F., Kingsman, A.J. & Kingsman, S.M. (1982) Sequence and structure of yeast phosphoglycerate kinase. EMBO J. 1, 1635-1640.
8. 8. Bernstein, B.E., Michels, P.A.M. & Hol, W.G.J. (1997). Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation. Nature 385, 275-278.
9. 9. Auerbach, G., Jacob, U., Grättinger, M., Schurig, H. & Jaenicke, R. (1997) Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima. J. Biol. Chem. 378, 327-329.
10. 10. Brandts, J.F., Halvorson, H.R. & Brennan, M. (1975) Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14, 4953-4963.
11. 11. Mayr, L.M. & Schmid, F.X. (1993) Kinetic-models for unfolding and refolding of ribonuclease-T (1) with substitution of cis-proline-39 by alanine. J. Mol. Biol. 231, 913-926.
12. 12. Weiner, M.P., Felts, K.A., Simcox, T.G. & Braman, J.C. (1993) A method for the site-directed mono-mutagenesis and multi-mutagenesis of double-stranded DNA. Gene 126, 35-41.
13. 13. Minard, P., Bowen, D.J., Hall, L., Littlechild, J.A. & Watson, H.C. (1990) Site-directed mutagenesis of aspartic acid 372 at the ATP binding site of yeast phosphoglycerate kinase: over expression and characterization of the mutant enzyme. Protein Eng. 3, 515-521.
14. 14. Gietz, R.D. & Schiestl, R.H. (1995) Transforming yeast with DNA. Methods Mol. Cell. Biol. 5, 255-269.
15. 15. Cooper, A. & Johnson, C.M. (1994) Differential Scanning Calorimetry. In: Methods in Molecular Biology, 22 Microscopy, Optical Spectroscopy and Macroscopic Techniques (Jones, C., Molloy, B. & Thomas, A.H., eds.), pp. 125-136. Humana Press, Totowa, NJ.
16. 16. Nojima, H., Ikai, A. & Noda, H. (1976) Anomalous fluorescence of yeast 3-phosphoglycerate kinase. Biochim. Biophys. Acta 427, 20-27.
17. 17. Longworth, J.W. (1971) In Excited States of Proteins and Nucleic Acids (Steiner, R.F. & Weinryb, I., eds.), pp. 319-484. Plenum Press, New York.
18. 18. Eftink, M.R. & Ghiron, C.A. (1976) Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry 15, 672-680.
19. 19. Missiakas, D., Betton, J.M., Minard, P. & Yon, J.M. (1990) Unfolding-refolding of the domains in yeast phosphoglycerate kinase: comparison with the isolated engineered domains. Biochemistry 29, 8683-8689.
20. 20. Garcia, P., Desmadril, M., Minard, P. & Yon, J.M. (1995) Evidence for residual structures in an unfolded form of yeast phosphoglycerate kinase. Biochemistry 34, 397-404.
21. 21. Evans, P.A., Topping, K.D., Woolfson, D.N. & Dobson, C.M. (1991) Hydrophobic clustering in nonactive states of a protein - interpretation of chemical shifts in NMR-spectra of denatured states of lysozyme. Proteins 9, 248-266.
22. 22. James, E., Wu, P.G., Stites, W. & Brand, L. (1992) Compact denatured state of a staphylococcal nuclease mutant by guanidinium chloride as determined by resonance energy transfer. Biochemistry 31, 10217-10225.
23. 23. Saab-Rincón, G., Froebe, C.L. & Matthews, C.R. (1993) Urea-induced unfolding of the alpha-subunit of tryptophan synthase - one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. Biochemistry 32, 13981-13990.
24. 24. Parker, M.J., Sessions, R.B., Badcoe, I.G. & Clarke, A.R. (1996) The development of tertiary interactions during the folding of a large protein. Folding Des. 1, 145-156.
25. 25. Bailey, J.M., Lin, L.-N., Brandts, J.F. & Mas, M.T. (1990) Substitution of a proline for alanine 183 in the hinge region of phosphoglycerate kinase: effects on catalysis, activation by sulphate, and thermal stability. J. Protein Chem. 9, 59-67.
26. 26. Johnson, M.J., Cooper, A. & Brown, A.J.P. (1991) A comparison of the reactivity and stability of wild type and His388-Gln mutant phosphoglycerate kinase from yeast. Eur. J. Biochem. 202, 1157-1164.
27. 27. Semisotnov, G.V., Vas, M., Chemeris, V.V., Kashparova, N.J., Kotova, N.V., Razgulyaev, O.I. & Sinev, M.A. (1991) Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragments. Eur. J. Biochem. 202, 1083-1089.
28. 28. Mas, M.T., Chen, H.H., Aisaka, K., Lin, L.N. & Brandts, J.F. (1995) Effects of C-terminal deletions on the conformational state and denaturation of phosphoglycerate kinase. Biochemistry 34, 7931-7940.
29. 29. Sherman, M.A., Chen, Y. & Mas, M.T. (1997) An engineered amino-terminal domain of yeast phosphoglycerate kinase with native-like structure. Protein Sci. 6, 882-891.
30. 30. Sherman, M.A., Dean, S.A., Mathiowetz, A.M. & Mas, M.T. (1991) Site-directed mutations of arginine 65 at the periphery of the active site cleft of yeast 3-phosphoglycerate kinase enhance the catalytic activity and eliminate anion-dependent activation. Protein Eng. 4, 935-940.
31. 31. Walker, P.A., Joao, H.C., Littlechild, J.A., Williams, R.J.P. & Watson, H.C. (1992) Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21. Eur J. Biochem. 207, 29-37.