Effect of a disulfide bond on mevalonate kinase

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 12, 2007, Pages 1571-1581

  Chu, Xiusheng ^a,b   Yu, Wenhua ^a   Wu, Long ^a   Liu, Xiaojun ^a   Li, Nan ^a   Li, Ding ^a  

^a CITY UNIVERSITY OF HONG KONG   (Hong Kong)

^b SHANDONG PEANUT RESEARCH INSTITUTE   (China)

Author keywords

Disulfide bond; Fluorescence; Mevalonate kinase; Mevalonate pathway; Thermal activity

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHOLESTEROL; CYSTEINE; DISULFIDE; ENZYME VARIANT; ISOPRENOID; MEVALONATE KINASE; PHOSPHOMEVALONATE KINASE; THIOL;

ARTICLE; CATALYSIS; CHOLESTEROL SYNTHESIS; CONFORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISULFIDE BOND; ENZYME ACTIVITY; FLUORESCENCE; METHANOCOCCUS JANNASCHII; MUTANT; NONHUMAN; PLANT; PRIORITY JOURNAL; RAT; TITRIMETRY; WILD TYPE;

AMINO ACID SEQUENCE; ANIMALS; CIRCULAR DICHROISM; DISULFIDES; GENE EXPRESSION; METHANOCOCCUS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; RATS; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY, AMINO ACID; SULFHYDRYL COMPOUNDS; TEMPERATURE;

ANIMALIA; METHANOCALDOCOCCUS JANNASCHII; RATTUS;

EID: 36848998781     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.09.004     Document Type: Article

References (55)

1. Buhaescu I., and Izzedine H. Mevalonate pathway: a review of clinical and therapeutical implications. Clin. Biochem. 40 (2007) 575-584
2. Swanson K.M., and Hohl R.J. Anti-cancer therapy: targeting the mevalonate pathway. Curr. Cancer Drug Targets 6 (2006) 15-37
3. Sgraja T., Smith T.K., and Hunter W.N. Structure, substrate recognition and reactivity of Leishmania major mevalonate kinase. BMC Struct. Biol. 7 (2007) 20
4. Eisenreich W., Bacher A., Arigoni D., and Rohdich F. Biosynthesis of isoprenoids via the non-mevalonate pathway. Cell. Mol. Life Sci. 61 (2004) 1401-1426
5. Contin A., Van der Heijden R., Lefeber A., and Verpoorte R. The iridoid glucoside secologanin is derived from the novel triose phosphate/pyruvate pathway in a Catharanthus roseus cell culture. FEBS Lett. 434 (1998) 413-416
6. Schulte A., Heijden R., and Verpoorte R. Purification and characterization of mevalonate kinase from suspension-cultured cells of Catharanthus roseus (L.) G. Don. Arch. Biochem. Biophys. 378 (2000) 287-298
7. Wright M.E., Virtamo J., Hartman A.M., Pietinen P., Edwards B.K., Taylor P.R., Huttunen J.K., and Albanes D. Effects of alpha-tocopherol and beta-carotene supplementation on upper aerodigestive tract cancers in a large, randomized controlled trial. Cancer 109 (2007) 891-898
8. Yan X.D., Li M., Yuan Y., Mao N., and Pan L.Y. Biological comparison of ovarian cancer resistant cell lines to cisplatin and Taxol by two different administrations. Oncol. Rep. 17 (2007) 1163-1169
9. Larsson S.C., Bergkvist L., Naslund I., Rutegard J., and Wolk A. Vitamin A, retinol, and carotenoids and the risk of gastric cancer: a prospective cohort study. Am. J. Clin. Nutr. 85 (2007) 497-503
10. Bishop R., Chambliss K., Hoffmann G., Tanaka R., and Gibson K. Characterization of the mevalonate kinase 5′- untranslated region provides evidence for coordinate regulation of cholesterol biosynthesis. Biochem. Biophys. Res. Commun. 242 (1998) 518-524
11. Tanaka R., Lee L., Schafer B., Kratunis V., Mohler W., Robinson G., and Mosley S. Molecular cloning of mevalonate kinase and regulation of its mRNA levels in rat liver. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 2872-2876
12. Hinson D., Chambliss K., Toth M., Tanaka R., and Gibson K. Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and nonsterol isoprene biosynthetic pathways. J. Lipid Res. 38 (1997) 2216-2223
13. Goldstein J., and Brown M. Regulation of the mevalonate pathway. Nature 343 (1990) 425-430
14. Rocco M., Caruso U., Waterham H., Picco P., Loy A., and Wanders R. Mevalonate kinase deficiency in a child with periodic fever and without hyperimmunoglobulinaemia D. J. Inherit. Metab. 24 (2001) 411-412
15. Houten S., Frenkel J., Kuis M., Wanders R., Poll-The B., and Waterham H. Molecular basis of classical mevalonic aciduria and the hyperimmunoglobulinaemia D and periodic fever syndrome: High frequency of 3 mutations in the mevalonate kinase gene. J. Inherit. Metab. Dis. 23 (2000) 367-370
16. Drenth J.P., Cuisset L., Grateau G., Vasseur C., van de Velde-Visser S.D., de Jong J.G., Beckmann J.S., van der Meer J.W., and Delpech M. Mutations in the gene encoding mevalonate kinase cause hyper-IgD and periodic fever syndrome. Nat. Genet. 22 (1999) 178-181
17. Houten S.M., Kuis W., Duran M., de Koning T.J., van Royen-Kerkhof A., Romeijn G.J., Frenkel J., Dorland L., de Barse M.M., Huijbers W.A., Rijkers G.T., Waterham H.R., Wanders R.J., and Poll-The B.T. Mutations in MVK, encoding mevalonate kinase, cause hyperimmunoglobulinaemia D and periodic fever syndrome. Nat. Genet. 22 (1999) 175-177
18. Quistad G., Cerf D., Schooley D., and Staal G. Fluoromevalonate acts as an inhibitor of insect juvenile hormone biosynthesis. Nature 289 (1981) 176-177
19. Yang D., Shipman L.W., Roessner C.A., Scott A.I., and Sacchettini J.C. Structure of the Methanococcus jannaschii mevalonate kinase, a member of the GHMP kinase superfamily. J. Biol. Chem. 277 (2002) 9462-9467
20. Fu Z.J., Wang M., Potter D., Miziorko H.M., and Kim J.J.P. The structure of a binary complex between a mammalian mevalonate kinase and ATP - insights into the reaction mechanism and human inherited disease. J. Biol. Chem. 277 (2002) 18134-18142
21. Andreassi J.L., Bilder P.W., Vetting M.W., Roderick S.L., and Leyh T.S. Crystal structure of the Streptococcus pneumoniae mevalonate kinase in complex with diphosphomevalonate. Protein Sci. 16 (2007) 983-989
22. Chu X., Liu X., Yau M., Leung Y.C., and Li D. Expression and purification of Arg196 and Lys272 mutants of mevalonate kinase from Methanococcus jannaschii. Protein Expr. Purif. 30 (2003) 210-218
23. Chu X., and Li D. Cloning, expression, and purification of His-tagged rat mevalonate kinase. Protein Exp. Purif. 27 (2003) 165-170
24. Chu X., and Li D. Expression, purification, and characterization of His20 mutants of rat mevalonate kinase. Protein Expr. Purif. 32 (2003) 75-82
25. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
26. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
27. Huang K., Scott A., and Bennett G. Overexpression, purification, and characterization of the thermostable mevalonate kinase from Methanococcus jannaschii. Protein Exp. Purif. 17 (1999) 33-40
28. Riener C.K., Kada G., and Gruber H.J. Quick measurement of protein sulfhydryls with Ellman′s reagent and with 4,4′-dithiodipyridine. Anal. Bioanal. Chem. 373 (2002) 266-276
29. Durrschmidt P., Mansfeld J., and Ulbrich-Hofmann R. Differentiation between conformational and autoproteolytic stability of the neutral protease from Bacillus stearothermophilus containing an engineered disulfide bond. Eur. J. Biochem. 268 (2001) 3612-3618
30. Colgrave M.L., and Craik D.J. Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: The importance of the cyclic cystine knot. Biochemistry 43 (2004) 5965-5975
31. Herdendorf T.J., and Miziorko H.M. Phosphomevalonate Kinase: functional investigation of the recombinant human enzyme. Biochemistry 45 (2006) 3235-3242
32. Mansfeld J., Vriend G., Dijkstra B.W., Veltman O.R., Burg B.V.D., Venema G., Ulbrich-Hofmann R., and Eijsink V.G. Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond. J. Biol. Chem. 272 (1997) 11152-11156
33. Riou C., Tourte Y., Lacroute F., and Karst F. Isolation and characterization of a cDNA encoding Arabidopsis thaliana mevalonate kinase by genetic complementation in yeast. Gene 148 (1994) 293-297
34. Oulmouden A., and Karst F. Nucleotide sequence of the ERG12 gene of Saccharomyces cerevisiae encoding mevalonate kinase. Curr. Genet. 19 (1991) 9-14
35. Schafer B.L., Bishop R.W., Kratunis V.J., Kalinowski S.S., Mosley S.T., Gibson K.M., and Tanaka R.D. Molecular cloning of human mevalonate kinase and identification of a missense mutation in the genetic disease mevalonic aciduria. J. Biol. Chem. 267 (1992) 13229-13238
36. Hansen R.E., Ostergaard H., and Winther J.R. Increasing the reactivity of an artificial dithiol-disulfide pair through modification of the electrostatic milieu. Biochemistry 44 (2005) 5899-5906
37. Ostergaard H., Henriksen A., Hansen F.G., and Winther J.R. Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein. EMBO J. 20 (2001) 5853-5862
38. Kihara M., Chatani E., Iwata K., Yamamoto K., Matsuura T., Nakagawa A., Naiki H., and Goto Y. Conformation of amyloid fibrils of beta2-microglobulin probed by tryptophan mutagenesis. J. Biol. Chem. 281 (2006) 31061-31069
39. Martinho J.M., Santos A.M., Fedorov A., Baptista R.P., Taipa M.A., and Cabral J.M. Fluorescence of the single tryptophan of cutinase: temperature and pH effect on protein conformation and dynamics. Photochem. Photobiol. 78 (2003) 15-22
40. Cowgill R.W. Fluorescence and protein structure. XI. Fluorescence quenching by disulfide and sulfhydryl groups. Biochim. Biophys. Acta 140 (1967) 37-44
41. Bujalowski W., and Klonowska M.M. Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DNAB protein. Interact. Fluoresc. Nucleotide Analogs Biochem. 32 (1993) 5888-5900
42. Cho Y.-K., Rios S.E., Kim J.-J.P., and Miziorko H.M. Investigation of invariant serine/threonine residues in mevalonate kinase. J. Biol. Chem. 276 (2001) 12573-12578
43. Krepkiy D., and Miziorko H.M. Identification of active site residues in mevalonate diphosphate decarboxylase: Implications for a family of phosphotransferases. Protein Sci. 13 (2004) 1875-1881
44. Krepkiy D.V., and Miziorko H.M. Investigation of the functional contributions of invariant serine residues in yeast mevalonate diphosphate decarboxylase. Biochemistry 44 (2005) 2671-2677
45. Runquist J.A., Narasimhan C., Wolff C.E., Koteiche H.A., and Miziorko H.M. Rhodobacter sphaeroides phosphoribulokinase: binary and ternary complexes with nucleotide substrate analogs and effectors. Biochemistry 35 (1996) 15049-15056
46. Arora K.K., Shenbagamurthi P., Fanciulli M., and Pedersen P.L. Glucose phosphorylation. Interaction of a 50-amino acid peptide of yeast hexokinase with trinitrophenyl ATP. J. Biol. Chem. 265 (1990) 5324-5328
47. Grubmeyer C., and Penefsky H.S. The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase. J. Biol. Chem. 256 (1981) 3718-3727
48. Vas M., Merli A., and Rossi G.L. Antagonistic binding of substrates to 3-phosphoglycerate kinase monitored by the fluorescent analogue 2′(3′)-0-(2,4,6-trinitrophenyl)adenosine 5′-triphosphate. Biochem. J. 301 (1994) 885-891
49. Broglie K.E., and Takahashi M. Fluorescence studies of threonine-promoted conformational transitions in aspartokinase I using the substrate analogue 2′(3′)-O-(2,4,6- trinitrophenyl)adenosine 5′-triphosphate. J. Biol. Chem. 258 (1983) 12940-12946
50. Hiratsuka T. Biological activities and spectroscopic properties of chromophoric and fluorescent analogs of adenine nucleoside and nucleotides, 2′,3′-O-(2,4,6-trinitro-cyclohexadienylidene) adenosine derivatives. Biochim. Biophys. Acta 719 (1982) 509-517
51. Meinhold D., Beach M., Shao Y., Osuna R., and Colon W. The location of an engineered inter-subunit disulfide bond in factor for inversion stimulation (FIS) affects the denaturation pathway and cooperativity. Biochemistry 45 (2006) 9767-9777
52. Cacciapuoti G., Moretti M.A., Forte S., Brio A., Camardella L., Zappia V., and Porcelli M. Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds. Eur. J. Biochem. 271 (2004) 4834-4844
53. Martensson L.G., Karlsson M., and Carlsson U. Dramatic stabilization of the native state of human carbonic anhydrase II by an engineered disulfide bond. Biochemistry 41 (2002) 15867-15875
54. Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
55. Chenna R., Sugawara H., Koike T., Lopez R., Gibson T.J., Higgins D.G., and Thompson J.D. Multiple sequence alignment with the clustal series of programs. Nucleic Acids Res. 31 (2003) 3497-3500