Glycinamide ribonucleotide transformylase undergoes pH-dependent dimerization

Journal of Molecular Biology

Volumn 262, Issue 5, 1996, Pages 746-755

  Mullen, Christine A ^a   Jennings, Patricia A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Absorbance difference spectroscopy; Dimerization; Dynamic light scattering; Folate; Glycinamide ribonucleotide transformylase

Indexed keywords

HISTIDINE; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; PROTON; TRYPTOPHAN; TYROSINE;

ARTICLE; COMPARATIVE STUDY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVITY; ENZYME CONFORMATION; FLUORESCENCE; IONIZATION; LIGHT SCATTERING; NONHUMAN; PH; PKA; PRIORITY JOURNAL; TITRIMETRY; ULTRAVIOLET SPECTROSCOPY;

EID: 0030580073     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0549     Document Type: Article

References (33)

1. Almassy, R. J., Janson, C. A., Kan, C.-C. & Hostomska, Z. (1992). Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase. Proc. Natl Acad. Sci. USA, 89, 6114-6118.
2. Appelt, K., Bacquet, R. J., Bartlett, C. A., Booth, L. J., Freer, S. T., Fuhry, M. A., Gehring, M. R., Herrmann, S. M., Howland, E. F., Janson, C. A., Jones, T. R., Kan, C.-C., Kathardekar, V., Lewis, K. K., Marzoni, G. P., Matthews, D. A., Mohr, C., Moomaw, E. W., Morse, C. A., Oatley, S. J., Ogden, R. C., Reddy, M. R., Reich, S. H., Schoettlin, W. S., Smith, W. W., Verney, M. D., Villafranca, J. E., Ward, W. R., Webber, S. Webber, S. E., Welsh, K. M. & White, J. (1991). Design of enzyme inhibitors using iterative protein crystallographic analysis. J. Med. Chem. 34, 1925-1934.
3. Baldwin, S. W., Tse, A., Gossett, S. L., Taylor, E. D., Rosowsky, A., Shih, C. & Moran, G. C. (1991). Structural features of 5,10-dideaza-5,6,7,8-tetrahydrofolate that determine inhibition of mammalian glycinamide ribonucleotide formyltransferase. Biochemistry, 30, 1997-2006.
4. Beardsley, G. P., Taylor, E. D., Grindey, G. B. & Moran, R. G. (1986). Deaza derivatives of tetrahydrofolic acid, a new class of folate antimetabolites. In Chemistry & Biology of Pteridines (Cooper, B. A. & Whitehead, V. M., eds), pp. 953-957, de Gruyter, Berlin, Germany.
5. Beardsley, G. P., Moroson, B. A., Taylor, E. D. & Moran, R. G. (1989). A new folate antimetabolite, 5,10-dideaza-5,6,7,8-tetrahydrofolate is a potent inhibitor of de novo purine synthesis. J. Biol. Chem. 264, 328-333.
6. Benkovic, S. J. & Young, M. (1987). Folate-dependent enzymes. In Enzyme Mechanisms (Page, M. I. & Williams, A., eds), pp. 429-441, The Royal Society of Chemistry, London.
7. Berman, E. M. & Werbel, L. M. (1991). The renewed potential for folate antagonists in contemporary cancer chemotherapy. J. Med. Chem. 34, 479-485.
8. Blaney, J. M., Mansch, C., Silipo, C. & Vittoria, A. (1984). Structure-activity relationships of dihydrofolate reductase inhibitors. Chem. Rev. 84, 333-407.
9. Chen, P., Schulze-Gahmen, U., Stura, E. A., Inglese, J., Johnson, D. L., Marolewski, A., Benkovic, S. J. & Wilson, I. A. (1992). Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 Å resolution. A target enzyme for chemotherapy. J. Mol. Biol. 227, 283-292.
10. Daubner, S. C. & Benkovic, S. J. (1985). Characterization of mammalian phosphoribosylglycineamide formyltransferase from transformed cells. Cancer Res. 45, 4990-4997.
11. Dev, I. K. & Harvey, R. J. (1978). N10-Formyltetrahydrofolate is the formyl donor for glycinamide ribonucleotide transformylase in Escherichia coli. J. Biol. Chem. 253, 4242-4244.
12. Donovan, J. W. (1973). Ultraviolet difference spectroscopy: new techniques and applications. Spectrophotometric titrations of functional groups in proteins. Methods Enzymol. 27, 497-525.
13. Finn, B. E., Chen, X., Jennings, P. A., Saalau-Bethel, S. M. & Matthews, C. R. (1987). Principles of protein stability. Part 1, reversible unfolding of proteins: kinetic and thermodynamic analysis. In Protein Engineering (Oxender, D. L. & Fox, C. F., eds), pp. 167-187, Liss, New York.
14. Gill, S. C. & von Hippel, P. H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
15. Herskovits, T. T. (1967). Difference spectroscopy. Methods Enzymol. 11, 748-775.
16. Inglese, J., Johnson, D. L., Shiau, A., Smith, J. M. & Benkovic, S. J. (1990). Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase. Biochemistry, 29, 1436-1443.
17. Klein, C., Chen, P., Arevalo, J. H., Stura, E. A., Marolewski, A., Warren, M. S., Benkovic, S. J. & Wilson, I. A. (1995). Towards structure-based drug design: crystal structure of a multisubstrate adduct complex of glycinamide ribonucleotide transformylase at 1.96 A resolution. J. Mol. Biol. 249, 153-175.
18. a. Biochemistry, 35, 1560-1570.
19. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
20. Maniatis, T., Fritsch, E. F. & Sambrook, J. (1982). Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
21. Miller, S., Lesk, A. M., Janin, J. & Chothia, C. (1987). The accessible surface area and stability of oligomeric proteins. Nature, 328, 834-836.
22. Montfort, W. R., Perry, K. M., Fauman, E. B., Finer-Moore, J. S., Maley, G. R., Hardy, L., Maley, F. & Stroud, R. M. (1990). Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate. Biochemistry, 29, 6964-6977.
23. Mullin, R. J., Keith, B. R., Bigham, E. C., Duch, D. S., Ferone, R., Heath, L. S., Singer, S., Waters, K. A. & Wilson, H. R. (1992). In vivo antitumor activity and metabolism of a series of 5-deazaacyclotetrahydrofolate (5-DACTHF) analogues. Biochem. Pharmacol. 43, 1627-1634.
24. Nichols, R., Weaver, C. D., Eisenstein, D., Blakley, R. L., Appleman, J., Huang, T.-H., Huang, F.-Y. & Howell, E. E. (1993). Titration of histidine 62 in R67 dihydrofolate reductase is linked to a tetramer ↔ two dimer equilibrium. Biochemistry, 32, 1695-1706.
25. Ray, S. M., Muggia, F. M., Leichman, C. G., Grunberg, S. M., Nelson, R. L., Dyke, R. W. & Moran, R. G. (1993). Phase I study of (6R)-5,10-dideazatetrahydrofolate: a folate antimetabolite inhibitory to de novo purine synthesis. J. Nat. Cancer Inst. 85, 1154-1159.
26. Rossman, M. G. & Argos, P. (1975). Chemical and biological evolution of a nucleotide-binding protein. Nature, 250, 194-199.
27. Schmid, F. X. (1989). Spectral methods of characterizing protein conformation and conformational changes. In Protein Structure: A Practical Approach (Creighton, T. E., ed.), pp. 251-285, IRL Press, Oxford.
28. Shih, C., Gossett, L. S., Worzalla, J. F., Rinzel, S. M., Grindey, G. B., Harrington, P. M. & Taylor, E. C. (1992). Synthesis and biological activity of acyclic analogues of 5,10-dideaza-5,6,7,8-tetrahydrofolic acid. J. Med. Chem. 35, 1109-1116.
29. Smith, G. K., Mueller, W. T., Slieker, L. J., DeBrosse, C. W. & Benkovic, S. J. (1982). Direct transfer of one-carbon units in the transformylations of de novo purine biosynthesis. Biochemistry, 21, 2870-2874.
30. Warren, M. S., Marolewski, A. E. & Benkovic, S. J. (1996). A rapid screen of active site mutants in glycinamide ribonucleotide transformylase. Biochemistry, 35, 8855-8862.
31. Webber, S. E., Bleckman, T. M., Attard, J., Deal, J. G., Katherdekar, V., Welsh, K. M., Webber, S., Janson, C. A., Matthews, D. A., Smith, W. W., Freer, S. T., Jordan, S. R., Bacquet, R. J., Howland, E. F., Booth, C. L. J., Ward, R. W., Hermann, S. M., White, J., Morse, C. A., Hillard, J. A. & Berlet, C. A. (1993). Design of thymidylate synthase inhibitor using protein crystal structures: the synthesis and biological evaluation of a novel class of 5-substituted quinazolinones. J. Med. Chem. 36, 733-746.
32. Yanari, S., & Bovey, F. A. (1960). Interpretation of the ultraviolet spectral changes of proteins. J. Biol. Chem. 235, 2818-2826.
33. Yang, J.-T., Wu, C.-S. C. & Martinez, H. M. (1986). Calculation of protein conformation from circular dichroism. Methods Enzmol. 130, 208-269.