Divalent metal requirements for catalysis and stability of the RNA triphosphatase from Trypanosoma cruzi

Molecular and Biochemical Parasitology

Volumn 150, Issue 1, 2006, Pages 83-95

  Massayuki Kikuti, Carlos ^a   Tersariol, Ivarne Luis S ^b   Schenkman, Sergio ^a  

^a FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

^b UNIVERSIDADE DE MOGI DAS CRUZES   (Brazil)

Author keywords

ATPase; Circular dichroism; Fluorescence; Kinetics; Manganese; RNA triphosphatase; Structure; Trypanosoma brucei; Trypanosoma cruzi

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CYSTEINE; MANGANESE; RNA TRIPHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHAGAS DISEASE; CIRCULAR DICHROISM; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STABILITY; FLUORESCENCE ANALYSIS; GEL PERMEATION CHROMATOGRAPHY; MICHAELIS MENTEN KINETICS; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; RNA CAPPING; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; TEMPERATURE DEPENDENCE; THERMOSTABILITY; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI;

ACID ANHYDRIDE HYDROLASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; CIRCULAR DICHROISM; COENZYMES; ENZYME STABILITY; FLUORESCENCE; HEAT; KINETICS; MANGANESE; MOLECULAR SEQUENCE DATA; RNA; SEQUENCE ALIGNMENT; TRYPANOSOMA BRUCEI BRUCEI; TRYPANOSOMA CRUZI;

EUKARYOTA; MAMMALIA; SACCHAROMYCES CEREVISIAE; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI;

EID: 33748329366     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2006.06.012     Document Type: Article

References (31)

1. Lima C.D., Wang L.K., and Shuman S. Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus. Cell (1999) 533-543
2. Shuman S. What messenger RNA capping tells us about eukaryotic evolution. Nat Rev Mol Cell Biol (2002) 619-625
3. Changela A., Ho C.K., Martins A., Shuman S., and Mondragon A. Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme. EMBO J (2001) 2575-2586
4. Changela A., Martins A., Shuman S., and Mondragon A. Crystal structure of baculovirus RNA triphosphatase complexed with phosphate. J Biol Chem (2005) 17848-17856
5. Shuman S. The mRNA capping apparatus as drug target and guide to eukaryotic phylogeny. Cold Spring Harb Symp Quant Biol (2001) 301-312
6. Tsukamoto T., Shibagaki Y., Imajoh-Ohmi S., et al. Isolation and characterization of the yeast mRNA capping enzyme beta subunit gene encoding RNA 5′-triphosphatase, which is essential for cell viability. Biochem Biophys Res Commun (1997) 116-122
7. Pei Y., Schwer B., Saiz J., Fisher R.P., and Shuman S. RNA triphosphatase is essential in Schizosaccharomyces pombe and Candida albicans. BMC Microbiol (2001) 29
8. Bisaillon M., and Bougie I. Investigating the role of metal ions in the catalytic mechanism of the yeast RNA triphosphatase. J Biol Chem (2003) 33963-33971
9. Martins A., and Shuman S. Mutational analysis of baculovirus capping enzyme Lef4 delineates an autonomous triphosphatase domain and structural determinants of divalent cation specificity. J Biol Chem (2001) 45522-45529
10. Bisaillon M., and Shuman S. Structure-function analysis of the active site tunnel of yeast RNA triphosphatase. J Biol Chem (2001) 17261-17266
11. Ho C.K., and Shuman S. Trypanosoma brucei RNA triphosphatase. Antiprotozoal drug target and guide to eukaryotic phylogeny. J Biol Chem (2001) 46182-46186
12. Gong C., Martins A., and Shuman S. Structure-function analysis of Trypanosoma brucei RNA triphosphatase and evidence for a two-metal mechanism. J Biol Chem (2003) 50843-50852
13. Bisaillon M., and Shuman S. Functional groups required for the stability of yeast RNA triphosphatase in vitro and in vivo. J Biol Chem (2001) 30514-30520
14. Medina-Acosta E., and Cross G.A. Rapid isolation of DNA from trypanosomatid protozoa using a simple 'mini-prep' procedure. Mol Biochem Parasitol (1993) 327-329
15. Gonzalez-Romo P., Sanchez-Nieto S., and Gavilanes-Ruiz M. A modified colorimetric method for the determination of orthophosphate in the presence of high ATP concentrations. Anal Biochem (1992) 235-238
16. Brooks S.P., and Storey K.B. Bound and determined: a computer program for making buffers of defined ion concentrations. Anal Biochem (1992) 119-126
17. Rinaldi T.A., Tersariol I.L., Dyszy F.H., et al. Protonation of two adjacent tyrosine residues influences the reduction of cytochrome c by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron. Free Radic Biol Med (2004) 802-810
18. Takagi T., Walker A.K., Sawa C., et al. The Caenorhabditis elegans mRNA 5′-capping enzyme. In vitro and in vivo characterization. J Biol Chem (2003) 14174-14184
19. Lee S.J., and Richardson C.C. Essential lysine residues in the RNA polymerase domain of the gene 4 primase-helicase of bacteriophage T7. J Biol Chem (2001) 49419-49426
20. Almeida P.C., Nantes I.L., Chagas J.R., et al. Cathepsin B activity regulation. Heparin-like glycosaminogylcans protect human cathepsin B from alkaline pH-induced inactivation. J Biol Chem (2001) 944-951
21. Chen Y.H., Yang J.T., and Martinez H.M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry (1972) 4120-4131
22. Mildvan A.S., and Cohn M. Kinetic and magnetic resonance studies of the pyruvate kinase reaction. II. Complexes of enzyme, metal, and substrates. J Biol Chem (1966) 1178-1193
23. 2+) on the hydrolytic activity of chloroplast ATPase. J Bioenerg Biomembr (2001) 93-98
24. Okimoto N., Yamanaka K., Ueno J., et al. Theoretical studies of the ATP hydrolysis mechanism of myosin. Biophys J (2001) 2786-2794
25. Bougie I., Parent A., and Bisaillon M. Thermodynamics of ligand binding by the yeast mRNA-capping enzyme reveals different modes of binding. Biochem J (2004) 411-420
26. Hubbard J.S., and Stadtman E.R. Regulation of glutamine synthetase. V. Partial purification and properties of glutamine synthetase from Bacillus licheniformis. J Bacteriol (1967) 1007-1015
27. London W.P., and Steck T.L. Kinetics of enzyme reactions with interaction between a substrate and a (metal) modifier. Biochemistry (1969) 1767-1779
28. +-ATPase by ATP. J Enzyme Inhib Med Chem (2004) 333-338
29. Li Z., and Neufeld G.J. Isolation and characterization of mitochondrial F(1)-ATPase from crayfish (Orconectes virilis) gills. Comp Biochem Physiol B Biochem Mol Biol (2001) 325-338
30. Hausmann S., Ho C.K., Schwer B., and Shuman S. An essential function of Saccharomyces cerevisiae RNA triphosphatase Cet1 is to stabilize RNA guanylyltransferase Ceg1 against thermal inactivation. J Biol Chem (2001) 36116-36124
31. Tschudi C., and Ullu E. Unconventional rules of small nuclear RNA transcription and cap modification in trypanosomatids. Gene Expr (2002) 3-16