Structural and kinetic properties of Bacillus subtilis S-adenosylmethionine synthetase expressed in Escherichia coli

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 12, 2008, Pages 1949-1958

  Kamarthapu, Venu ^a   Rao, Khareedu Venkateswara ^a   Srinivas, P N B S ^b   Reddy, G Bhanuprakash ^b   Reddy, Vudem Dashavantha ^a  

^a OSMANIA UNIVERSITY   (India)

^b NATIONAL INSTITUTE OF NUTRITION   (India)

Author keywords

Bacillus subtilis; Heterologus host; metE; S adenosylmethionine synthetase; Urea induced unfolding

Indexed keywords

ADENOSINE TRIPHOSPHATE; DIMER; MAGNESIUM; METHIONINE; METHIONINE ADENOSYLTRANSFERASE; MONOMER; POTASSIUM; S ADENOSYLMETHIONINE; TETRAMER; UREA;

ARTICLE; BACILLUS SUBTILIS; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ESCHERICHIA COLI; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; GENE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FOLDING; S ADENOSYLMETHIONINE SYNTHETASE GENE;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; CATALYTIC DOMAIN; ESCHERICHIA COLI; GENE EXPRESSION; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; KINETICS; MAGNESIUM; METHIONINE ADENOSYLTRANSFERASE; POTASSIUM; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; UREA;

BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 54549089920     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.06.006     Document Type: Article

References (48)

1. Cantoni G.L. S-adenosylmethionine; a new intermediate formed enzymatically from l-methionine and adenosinetriphosphate. J Biol Chem 204 (1953) 403-416
2. Mudd S.H., and Cantoni G.L. Activation of methionine for transmethylation. III. The methionine-activating enzyme of Bakers' yeast. J Biol Chem 231 (1958) 481-492
3. Takusagawa F., Kamitori S., Misaki S., and Markham G.D. Crystal structure of S-adenosylmethionine synthetase. J Biol Chem 271 (1996) 136-147
4. Chiang P.K., Gordon R.K., Tal J., Zeng G.C., Doctor B.P., Pardhasaradhi K., and McCann P.P. S-adenosylmethionine and methylation. FASEB J 10 (1996) 471-480
5. Bottiglieri T. S-adenosyl-l-methionine (SAMe): from the bench to the bedside-molecular basis of a pleiotrophic molecule. Am J Clin Nutr 76 (2002) 1151S-1157S
6. Fontecave M., Atta M., and Mulliez E. S-adenosylmethionine: nothing goes to waste. Trends Biochem Sci 29 (2004) 243-249
7. Pascale R.M., Marras V., Simile M.M., Daino L., Pinna G., Bennati S., Carta M., Seddaiu M.A., Massarelli G., and Feo F. Chemoprevention of rat liver carcinogenesis by S-adenosyl-l-methionine: a long-term study. Cancer Res 52 (1992) 4979-4986
8. Pegg A.E. Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy. Cancer Res 48 (1988) 759-774
9. Markham G.D., Hafner E.W., Tabor C.W., and Tabor H. S-adenosylmethionine synthetase from Escherichia coli. J Biol Chem 255 (1980) 9082-9092
10. Chiang P.K., and Cantoni G.L. Activation of methionine for transmethylation. Purification of the S-adenosylmethionine synthetase of bakers' yeast and its separation into two forms. J Biol Chem 252 (1977) 4506-4513
11. Porcelli M., Cacciapuoti G., Carteni-Farina M., and Gambacorta A. S-adenosylmethionine synthetase in the thermophilic archaebacterium Sulfolobus solfataricus. Purification and characterization of two isoforms. Eur J Biochem 177 (1988) 273-280
12. Reguera R.M., Balana-Fouce R., Perez-Pertejo Y., Fernandez F.J., Garcia-Estrada C., Cubria J.C., Ordonez C., and Ordonez D. Cloning expression and characterization of methionine adenosyltransferase in Leishmania infantum promastigotes. J Biol Chem 277 (2002) 3158-3167
13. Sullivan D.M., and Hoffman J.L. Fractionation and kinetic properties of rat liver and kidney methionine adenosyltransferase isozymes. Biochemistry 22 (1983) 1636-1641
14. Kotb M., and Kredich N.M. S-adenosylmethionine synthetase from human lymphocytes. Purification and characterization. J Biol Chem 260 (1985) 3923-3930
15. González B., Pajares M.A., Hermoso J.A., Alvarez L., Garrido F., Sufrin J.R., and Sanz-Aparicio J. The crystal structure of tetrameric methionine adenosyltransferase from rat liver reveals the methionine-binding site. J Mol Biol 300 (2000) 363-375
16. Gasset M., Alfonso C., Neira J.L., Rivas G., and Pajares M.A. Equilibrium unfolding studies of the rat liver methionine adenosyltransferase III, a dimeric enzyme with intersubunit active sites. Biochem J 361 (2002) 307-315
17. Yocum R.R., Perkins J.B., Howitt C.L., and Pero J. Cloning and characterization of the metE gene encoding S-adenosylmethionine synthetase from Bacillus subtilis. J Bacteriol 178 (1996) 4604-4610
18. Creighton T.E. Protein folding. Biochem J 270 (1990) 1-16
19. Reddy G.B., Srinivas V.R., Ahmad N., and Surolia A. Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity. Implications in protein folding and legume lectin oligomerization. J Biol Chem 274 (1999) 4500-4503
20. Jaenicke R. Protein folding: local structures, domains, subunits, and assemblies. Biochemistry 30 (1991) 3147-3161
21. Neet K.E., and Timm D.E. Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation. Protein Sci 3 (1994) 2167-2174
22. Batey S., Scott K.A., and Clarke J. Complex folding kinetics of a multidomain protein. Biophys J 90 (2006) 2120-2130
23. Jaenicke R., and Rudolph R. In: Creighton T.E. (Ed). Protein Structure: a Practical Approach (1989), IRL Press (Oxford University, Press), Oxford 191-224
24. Price N.C. Assembly of multi-subunit structures. Mechanisms of protein folding (1994), Oxford University Press, New York 160-193
25. Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., and Struhl K. Current Protocols in Molecular Biology Vo1. 1 (1993), Greene Publishing Associates, Inc. and John Wiley & Sons, Inc., USA 16.2.1-16.2.11
26. J. Sambrook, E.F. Fritsch, T. Manniatis, Cold Spring Harbor Laboratories, Cold Spring Harbor, New York,; Vol. 1, 2 and 3, 2001.
27. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
28. 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
29. Berger B.J., and Knodel M.H. Characterisation of methionine adenosyltransferase from Mycobacterium smegmatis and M. tuberculosis. BMC Microbiol 3 (2003) 12
30. Kim D.J., Huh J.H., Yang Y.Y., Kang C.M., Lee I.H., Hyun C.G., Hong S.K., and Suh J.W. Accumulation of S-adenosyl-l-methionine enhances production of actinorhodin but inhibits sporulation in Streptomyces lividans TK23. J Bacteriol 185 (2003) 592-600
31. Pegg A.E. Recent advances in the biochemistry of polyamines in eukaryotes. Biochem J 234 (1986) 249-262
32. Grillo M.A., and Colombatto S. S-adenosylmethionine and radical-based catalysis. Amino Acids 32 (2007) 197-202
33. McDaniel B.A., Grundy F.J., Kurlekar V.P., Tomsic J., and Henkin T.M. Identification of a mutation in the Bacillus subtilis S-adenosylmethionine synthetase gene that results in derepression of S-box gene expression. J Bacteriol 188 (2006) 3674-3681
34. Hilti N., Graub R., Jorg M., Arnold P., Schweingruber A.M., and Schweingruber M.E. Gene sam1 encoding adenosylmethionine synthetase: effects of its expression in the fission yeast Schizosaccharomyces pombe. Yeast 16 (2000) 1-10
35. Ochi K., and Freese E. A decrease in S-adenosylmethionine synthetase activity increases the probability of spontaneous sporulation. J Bacteriol 152 (1982) 400-410
36. Ferrer M., Chernikova T.N., Yakimov M.M., Golyshin P.N., and Timmis K.N. Chaperonins govern growth of Escherichia coli at low temperatures. Nat Biotechnol 21 (2003) 1266-1267
37. Weickert M.J., Doherty D.H., Best E.A., and Olins P.O. Optimization of heterologous protein production in Escherichia coli. Curr Opin Biotechnol 7 (1996) 494-499
38. Sorensen H.P., and Mortensen K.K. Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb Cell Fact 4 (2005) 1
39. Street T.O., Bolen D.W., and Rose G.D. A molecular mechanism for osmolyte-induced protein stability. Proc Natl Acad Sci U S A 103 (2006) 13997-14002
40. Komoto J., Yamada T., Takata Y., Markham G.D., and Takusagawa F. Crystal structure of the S-adenosylmethionine synthetase ternary complex: a novel catalytic mechanism of S-adenosylmethionine synthesis from ATP and Met. Biochemistry 43 (2004) 1821-1831
41. Eftink M.R., and Ionescu R. Thermodynamics of protein unfolding: questions pertinent to testing the validity of the two-state model. Biophys Chem 64 (1997) 175-197
42. Dill K.A. Dominant forces in protein folding. Biochemistry 29 (1990) 7133-7155
43. Privalov P.L. Stability of proteins: small globular proteins. Adv Protein Chem 33 (1979) 167-241
44. Eftink M.R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys J 66 (1994) 482-501
45. Chatterjee A., and Mandal D.K. Denaturant-induced equilibrium unfolding of concanavalin A is expressed by a three-state mechanism and provides an estimate of its protein stability. Biochim Biophys Acta 1648 (2003) 174-183
46. Kumar M.S., Reddy P.Y., Sreedhar B., and Reddy G.B. αB-crystallin-assisted reactivation of glucose-6-phosphate dehydrogenase upon refolding. Biochem J 391 (2005) 335-341
47. Kelly S.M., and Price N.C. The application of circular dichroism to studies of protein folding and unfolding. Biochim Biophys Acta 1338 (1997) 161-185
48. Sanchez del Pino M.M., Perez-Mato I., Sanz J.M., Mato J.M., and Corrales F.J. Folding of dimeric methionine adenosyltransferase III: identification of two folding intermediates. J Biol Chem 277 (2002) 12061-12066