Probing the roles of non-homologous insertions in the N-terminal domain of Plasmodium falciparum hydroxymethylpterin pyrophosphokinase-dihydropteroate synthase

Molecular and Biochemical Parasitology

Volumn 168, Issue 2, 2009, Pages 135-142

  Rattanachuen, Woraphol ^a   Jönsson, Maria ^b   Swedberg, Göte ^b   Sirawaraporn, Worachart ^a  

^a MAHIDOL UNIVERSITY   (Thailand)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

Bifunctional enzyme; Dihydropteroate synthase; Drug target; Hydroxymethylpterin pyrophosphokinase; Malaria; Plasmodium falciparum; Plasmodium specific inserts

Indexed keywords

AMINO ACID; DIHYDROPTEROATE SYNTHASE; HYDROXYMETHYLPTERIN PYROPHOSPHOKINASE; PHOSPHOTRANSFERASE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL STRAIN; CATALYSIS; CONTROLLED STUDY; ENZYME KINETICS; ESCHERICHIA COLI; GENE DELETION; GENE INSERTION; MUTANT; NONHUMAN; NUCLEOTIDE SEQUENCE; PLASMID; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; DIHYDROPTEROATE SYNTHASE; DIPHOSPHOTRANSFERASES; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, INSERTIONAL; MUTANT PROTEINS; PLASMODIUM FALCIPARUM; SEQUENCE ALIGNMENT; SEQUENCE DELETION;

PLASMODIUM FALCIPARUM;

EID: 70349289077     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2009.07.005     Document Type: Article

References (40)

1. Nzila A., Ward S.A., Marsh K., Sims P.F.G., and Hyde J.E. Comparative folate metabolism in humans and malaria parasites (part II): activities as yet untargeted or specific to Plasmodium. Trends Parasitol 21 (2005) 334-339
2. Shen F., Ross J., Wang X., and Ratnam M. Identification of a novel folate receptor, a truncated receptor, and receptor type beta in hematopoietic cells: cDNA cloning, expression, immunoreactivity, and tissue specificity. Biochemistry 33 (1994) 1209-1215
3. Wang P., Wang Q., Sims P.F.G., and Hyde J.E. Characterisation of exogenous folate transport in Plasmodium falciparum. Mol Biochem Parasitol 154 (2007) 40-51
4. Nzila A. Inhibitors of de novo folate enzymes in Plasmodium falciparum. Drug Discov Today 11 (2006) 939-944
5. Wongsrichanalai C., Pickard A.L., Wernsdorfer W.H., and Meshnick S.R. Epidemiology of drug-resistant malaria. Lancet Infect Dis 2 (2002) 209-218
6. Triglia T., Menting J.G., Wilson C., and Cowman A.F. Mutations in dihydropteroate synthase are responsible for sulfone and sulfonamide resistance in Plasmodium falciparum. Proc Natl Acad Sci USA 94 (1997) 13944-13949
7. Mutabingwa T., Nzila A., Mberu E., et al. Chlorproguanil-dapsone for treatment of drug-resistant falciparum malaria in Tanzania. Lancet 358 (2001) 1218-1223
8. Winstanley P. Chlorproguanil-dapsone (LAPDAP) for uncomplicated falciparum malaria. Trop Med Int Health 6 (2001) 952-954
9. Triglia T., and Cowman A.F. Primary structure and expression of the dihydropteroate synthetase gene of Plasmodium falciparum. Proc Natl Acad Sci USA 91 (1994) 7149-7153
10. Brooks D.R., Wang P., Read M., Watkins W.M., Sims P.F., and Hyde J.E. Sequence variation of the hydroxymethyldihydropterin pyrophosphokinase: dihydropteroate synthase gene in lines of the human malaria parasite, Plasmodium falciparum, with differing resistance to sulfadoxine. Eur J Biochem 224 2 (1994) 397-405
11. Salcedo E., Cortese J.F., Plowe C.V., Sims P.F., and Hyde J.E. A bifunctional dihydrofolate synthetase-folylpolyglutamate synthetase in Plasmodium falciparum identified by functional complementation in yeast and bacteria. Mol Biochem Parasitol 112 (2001) 239-252
12. Ivanetich K.M., and Santi D.V. Bifunctional thymidylate synthase-dihydrofolate reductase in protozoa. FASEB J 4 (1990) 1591-1597
13. Bzik D.J., Li W.-B., Horii T., and Inselburg J. Molecular cloning and sequence analysis of the Plasmodium falciparum dihydrofolate reductase-thymidylate synthase gene. Proc Natl Acad Sci USA 84 (1987) 8360-8364
14. Anderson A.C. Two crystal structures of dihydrofolate reductase-thymidylate synthase from Cryptosporidium hominis reveal protein-ligand interactions including a structural basis for observed antifolate resistance. Acta Crystallogr Sec F: Struct Biol Cryst Commun 61 (2005) 258-262
15. Grumont R., Sirawaraporn W., and Santi D.V. Heterologous expression of the bifunctional thymidylate synthase-dihydrofolate reductase from Leishmania major. Biochemistry 27 (1988) 3776-3784
16. Herrmann L., Bockau U., Tiedtke A., Hartmann M.W., and Weide T. The bifunctional dihydrofolate reductase thymidylate synthase of Tetrahymena thermophila provides a tool for molecular and biotechnology applications. BMC Biotechnol 6 (2006) 21
17. Lawrence M.C., Iliades P., Fernley R.T., Berglez J., Pilling P.A., and Macreadie I.G. The three-dimensional structure of the bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/dihydropteroate synthase of Saccharomyces cerevisiae. J Mol Biol 348 (2005) 655-670
18. Mouillon J.M., Ravanel S., Douce R., and Rébeillé F. Folate synthesis in higher-plant mitochondria: coupling between the dihydropterin pyrophosphokinase and the dihydropteroate synthase activities. Biochem J 363 (2002) 313-319
19. Miles E.W., Rhee S., and Davies D.R. The molecular basis of substrate channeling. J Biol Chem 274 (1999) 12193-12196
20. Müller S., Da'dara A., Lüersen K., et al. In the human malaria parasite Plasmodium falciparum, polyamines are synthesized by a bifunctional ornithine decarboxylase, S-adenosylmethionine decarboxylase. J Biol Chem 275 (2000) 8097-8102
21. Gilberger T.W., Schirmer R.H., Walter R.D., and Müller S. Deletion of the parasite-specific insertions and mutation of the catalytic triad in glutathione reductase from chloroquine-sensitive Plasmodium falciparum 3D7. Mol Biochem Parasitol 107 (2000) 169-179
22. Clarke J.L., Scopes D.A., Sodeinde O., and Mason P.J. Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase. A novel bifunctional enzyme in malaria parasites. Eur J Biochem 268 (2001) 2013-2019
23. Carucci D.J., Witney A.A., Muhia D.K., et al. Guanylyl cyclase activity associated with putative bifunctional integral membrane proteins in Plasmodium falciparum. J Biol Chem 275 (2000) 22147-22156
24. Merckx A., Echalier A., Langford K., et al. Structures of P. falciparum protein kinase 7 identify an activation motif and leads for inhibitor design. Structure 16 (2008) 228-238
25. Birkholtz L.M., Wrenger C., Joubert F., Wells G.A., Walter R.D., and Louw A.I. Parasite-specific inserts in the bifunctional S-adenosylmethionine decarboxylase/ornithine decarboxylase of Plasmodium falciparum modulate catalytic activities and domain interactions. Biochem J 377 (2004) 439-448
26. Fermér C., and Swedberg G. Adaptation to sulfonamide resistance in Neisseria meningitidis may have required compensatory changes to retain enzyme function: kinetic analysis of dihydropteroate synthases from N. meningitidis expressed in a knockout mutant of Escherichia coli. J Bacteriol 179 (1997) 831-837
27. Jönsson M., and Swedberg G. Hydroxymethyldihydropterin pyrophosphokinase from Plasmodium falciparum complements a folK-knockout mutant in E. coli when expressed as a separate polypeptide detached from dihydropteroate synthase. Mol Biochem Parasitol 140 (2005) 123-125
28. Xiao B., Shi G., Chen X., Yan H., and Ji X. Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents. Structure 7 (1999) 489-496
29. Achari A., Somers D.O., Champness J.N., Bryant P.K., Rosemond J., and Stammers D.K. Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase. Nat Struct Biol 4 (1997) 490-497
30. Babaoglu K., Qi J., Lee R.E., and White S.W. Crystal structure of 7,8-dihydropteroate synthase from Bacillus anthracis: mechanism and novel inhibitor design. Structure 12 (2004) 1705-1717
31. Baca A.M., Sirawaraporn R., Turley S., Sirawaraporn W., and Hol W.G. Crystal structure of Mycobacterium tuberculosis 6-hydroxymethyl-7,8-dihydropteroate synthase in complex with pterin monophosphate: new insight into the enzymatic mechanism and sulfa-drug action. J Mol Biol 302 (2000) 1193-1212
32. Hampele I.C., D'Arcy A., Dale G.E., et al. Structure and function of the dihydropteroate synthase from Staphylococcus aureus. J Mol Biol 268 (1997) 21-30
33. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of structural information in progressive multiple sequence alignments using 3D-Coffee. Nucleic through sequence weighting, position specific gap penalties and weight matrix choice. Nucl Acids Res 22 (1994) 4673-4680
34. Sambrook J., and Russell D.W. Molecular cloning: a laboratory manual. 3rd ed. (2000), Cold Spring Laboratory Press, Cold Spring Harbor
35. Kasekarn W., Sirawaraporn R., Chahomchuen T., Cowman A.F., and Sirawaraporn W. Molecular characterization of bifunctional hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium falciparum. Mol Biochem Parasitol 137 (2004) 43-53
36. Testani J.M., Dabelic R., and Rasche M.E. Chemical reduction of pterins to dihydropterins as substrates for enzymatic reactions. Anal Chem 358 (2006) 20-24
37. Nopponpunth V., Sirawaraporn W., Greene P.J., and Santi D.V. Cloning and expression of Mycobacterium tuberculosis and Mycobacterium leprae dihydropteroate synthase in Escherichia coli. J Bacteriol 181 (1999) 6814-6821
38. Korsinczky M., Fischer K., Chen N., Baker J., Rieckmann K., and Cheng Q. Sulfadoxine resistance in Plasmodium vivax is associated with a specific amino acid in dihydropteroate synthase at the putative sulfadoxine-binding site. Antimicrob Agents Chemother 48 6 (2004) 2214-2222
39. de Beer T.A., Louw A.I., and Joubert F. Elucidation of sulfadoxine resistance with structural models of the bifunctional Plasmodium falciparum dihydropterin pyrophosphokinase-dihydropteroate synthase. Bioorg Med Chem 14 (2006) 4433-4443
40. Shallom S., Zhang K., Jiang L., and Rathod P.K. Essential protein-protein interactions between Plasmodium falciparum thymidylate synthase and dihydrofolate reductase domains. J Biol Chem 274 (1999) 37781-37786