Effects of mutation at methionine-42 of Escherichia coli dihydrofolate reductase on stability and function: Implication of hydrophobic interactions

Journal of Biochemistry

Volumn 137, Issue 5, 2005, Pages 643-652

  Ohmae, Eiji ^a   Fukumizu, Yukari ^a   Iwakura, Masahiro ^b   Gekko, Kunihiko ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

Dihydrofolate reductase; Enzyme function; Hydrophobic interaction; Mutation at methionine 42; Structural stability

Indexed keywords

ALANINE; AMINO ACID; CYSTEINE; DIHYDROFOLATE REDUCTASE; GLUTAMINE; GLYCINE; HISTIDINE; ISOLEUCINE; LEUCINE; METHIONINE; PROLINE; SERINE; THREONINE; TRYPTOPHAN; TYROSINE; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; CELL INTERACTION; CIRCULAR DICHROISM; ENZYME STABILITY; ESCHERICHIA COLI; GENE MUTATION; HYDROPHOBICITY; NONHUMAN; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; SPECTROSCOPY; STEADY STATE; WILD TYPE;

CIRCULAR DICHROISM; ENZYME STABILITY; ESCHERICHIA COLI; HEAT; HYDROPHOBICITY; KINETICS; METHIONINE; MODELS, MOLECULAR; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; TETRAHYDROFOLATE DEHYDROGENASE;

ESCHERICHIA COLI;

EID: 21044447962     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvi079     Document Type: Article

References (35)

1. Sawaya, M.R. and Kraut, J. (1997) Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36, 586-603
2. Kitahara, R., Sareth, S., Yamada, H., Ohmae, E., Gekko, K., and Akasaka, K. (2000) High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase. Biochemistry 39, 12789-12795
3. Gekko, K., Yamagami, K., Kunori, Y., Ichihara, S., Kodama, M., and Iwakura, M. (1993) Effects of point mutation in a flexible loop on the stability and enzymatic function of Escherichia coli dihydrofolate reductase. J. Biochem. 113, 74-80
4. Gekko, K., Kunori, Y., Takeuchi, H., Ichihara, S., and Kodama, M. (1994) Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: important roles of a flexible loop in the stability and function. J. Biochem. 116, 34-41
5. Cameron, C.E. and Benkovic, S.J. (1997) Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant. Biochemistry 36, 15792-15800
6. Ohmae, E., Iriyama, K., Ichihara, S., and Gekko, K. (1996) Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function. J. Biochem. 119, 703-710
7. Ohmae, E., Ishimura, K., Iwakura, M., and Gekko, K. (1998) Effects of point mutations at the flexible loop alanine-145 of Escherichia coli dihydrofolate reductase on its stability and function. J. Biochem. 123, 839-846
8. Ohmae, E., Iriyama, K., Ichihara, S., and Gekko, K. (1998) Nonadditive effects of double mutations at the flexible loops, glycine-67 and glycine-121, of Escherichia coli dihydrofolate reductase on its stability and function. J. Biochem. 123, 33-41
9. Gekko, K., Kamiyama, T., Ohmae, E., and Katayanagi, K. (2000) Single amino acid substitutions in flexible loops can induce large compressibility changes in dihydrofolate reductase. J. Biochem. 128, 21-27
10. Yamamoto, T., Izumi, S., Ohmae, E., and Gekko, K. (2004) Mass spectrometry of hydrogen/deuterium exchange of Escherichia coli dihydrofolate reductase: effects of loop mutations. J. Biochem. 135, 487-194
11. Rajagopalan, P.T.R., Lutz, S., and Benkovic, S.J. (2002) Coupling interactions of distal residues enhance dihydrofolate reductase catalysis: mutational effects on hydride transfer rates. Biochemistry 41, 12618-12628
12. Shaw, D., Odom, J.D., and Dunlap R.B. (1999) High expression and steady-state kinetic characterization of methionine site-directed mutants of Escherichia coli methionyl- and selenome-thionyl-dihydrofolate reductase. Biochim. Biophys. Acta 1429, 401-110
13. Iwakura, M., Jones, B.E., Luo, J., and Matthews, C.R. (1995) A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase gene from Escherichia coli. J. Biochem. 117, 480-188
14. Fierke, C.A., Johnson, K.A., and Benkovic, S.J. (1987) Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry 26, 4085-1092
15. Ohmae, E., Sasaki, Y., and Gekko, K. (2001) Effects of five-tryptophan mutations on structure, stability and function of Escherichia coli dihydrofolate reductase. J. Biochem. 130, 439-447
16. Pace, C.N. (1985) Determination and analysis of urea and guanidine hydrochloride denaturation curves in Methods Enzymol. (Hirs, C.H.W. and Timasheff, S.N., eds.) Vol. 131, pp. 267-280, Academic Press, New York
17. Williams, J.W., Morrison, J.F., and Duggleby, R.G. (1979) Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductase. Biochemistry 18, 2567-2573
18. Penner, M.H. and Frieden, C. (1985) Substrate induced hysteresis in the activity of Escherichia coli dihydrofolate reductase. J. Biol. Chem. 260, 5366-5369
19. Stone, S.R. and Morrison, J.F. (1982) Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli. Biochemistry 21, 3757-3765
20. Kuwajima, K., Garvey, E.P., Finn, B.E., Matthews, C.R., and Sugai, S. (1991) Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry 30, 7693-7703
21. Ohmae, E., Kurumiya, T., Makino, S., and Gekko, K. (1996) Acid and thermal unfolding of Escherichia coli dihydrofolate reductase. J. Biochem. 120, 946-953
22. Ahrweiler, P.M. and 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
23. Arnold, G.E., Day, L.A., and Dunker, A.K. (1992) Tryptophan contributions to the unusual circular dichroism of fd bacteriophage. Biochemistry 31, 7948-7956
24. Vuilleumier, S., Sancho, J., Loewenthal, R., and Fersht, A.R. (1993) Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains. Biochemistry 32, 10303-10313
25. Grishina, I.B. and Woody, R.W. (1994) Contributions of tryptophan side chains to the circular dichroism of globular proteins: exciton couplets and coupled oscillators. Faraday Discuss. 99, 245-262
26. Shellman, J.A. (1978) Solvent denaturation. Biopolymers 17, 1305-1322
27. Pace, C.N., Laurents, D.V., and Thomson, J.A. (1990) pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry 29, 2564-2572
28. Yutani, K., Ogasahara, K., Tsujita, T., and Sugino, Y. (1987) Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase α subunit. Proc. Natl Acad. Sci. USA 84, 4441-4444
29. Matsumura, M., Becktel, W.J., and Matthews, B.W. (1988) Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature 334, 406-410
30. Matsumura, M., Yahanda, S., Yasumura, S., Yutani, K., and Aiba, S. (1988) Role of tyrosine-80 in the stability of kanamycin nucleotidyltransferase analyzed by site-directed mutagenesis. Eur. J. Biochem. 171, 715-720
31. Kellis, J.T. Jr., Nyberg, K., and Fersht, A.R. (1989) Energetics of complementary side-chain packing in a protein hydrophobic core. Biochemistry 28, 4914-4922
32. Kauzmann, W. (1959) Some factors in the interpretation of protein denaturation. Adv. Protein Chem. 14, 1-63
33. Nozaki, Y. and Tanford, C. (1971) The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J. Biol. Chem. 246, 2211-2217
34. Zamyatnin, A.A. (1984) Amino acid, peptide, and protein volume in solution. Annu. Rev. Biophys. Bioeng. 13, 145-165
35. Bolin, J.T., Filman, D.J., Matthews, D.A., Hamlin, R.C., and Kraut, J. (1982) Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J. Biol. Chem. 257, 13650-13662