Over-expression in Escherichia coli, functional characterization and refolding of rat dimethylglycine dehydrogenase

Protein Expression and Purification

Volumn 37, Issue 2, 2004, Pages 434-442

  Brizio, Carmen ^a,c   Brandsch, Roderich ^c   Bufano, Daniela ^a   Pochini, Lorena ^d   Indiveri, Cesare ^d   Barile, Maria ^a,b  

^a UNIVERSITY OF BARI   (Italy)

^b CNR   (Italy)

^c UNIVERSITY OF FREIBURG   (Germany)

^d UNIVERSITY OF CALABRIA   (Italy)

Author keywords

Dimethylglycine dehydrogenase; FAD; Flavinylation; Flavoprotein; Mitochondria; Refolding

Indexed keywords

DIMETHYLGLYCINE; DIMETHYLGLYCINE DEHYDROGENASE; DMGDH PROTEIN, RAT; DRUG DERIVATIVE; HYBRID PROTEIN; MITOCHONDRIAL PROTEIN; N DEMETHYLASE; NICKEL; RECOMBINANT PROTEIN; SARCOSINE;

ANIMAL; ARTICLE; BIOCHEMISTRY; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; LIVER; METABOLISM; METHODOLOGY; PH; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; RAT; WESTERN BLOTTING;

ANIMALS; BIOCHEMISTRY; BLOTTING, WESTERN; DIMETHYLGLYCINE DEHYDROGENASE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; LIVER; MITOCHONDRIAL PROTEINS; NICKEL; OXIDOREDUCTASES, N-DEMETHYLATING; PLASMIDS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RATS; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; SARCOSINE;

ESCHERICHIA COLI;

EID: 4444224306     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.06.011     Document Type: Article

References (32)

1. Edmondson D.E., Newton-Vinson P. The covalent FAD of monoamine oxidase: structural and functional role and mechanism of the flavinylation reaction. Antioxid. Redox Signal. 3:2001;789-806
2. Mewies M., McIntire W.S., Scrutton N.S. Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: the current states of affairs. Protein Sci. 7:1998;7-20
3. Decker K., Brandsch R. Determining covalent flavinylation. Methods Enzymol. 280:1997;413-423
4. Wittwer A.J., Wagner C. Identification of folate binding protein of mitochondria as dimethylglycine dehydrogenase. Proc. Natl. Acad. Sci. USA. 77:1980;4484-4488
5. Wittwer A.J., Wagner C. Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Purification and folate-binding characteristics. J. Biol. Chem. 256:1981;4102-4108
6. Wittwer A.J., Wagner C. Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Flavoprotein nature and enzymatic properties of the purified proteins. J. Biol. Chem. 256:1981;4109-4115
7. Wagner C. Cellular folate binding proteins; function and significance. Annu. Rev. Nutr. 2:1982;229-248
8. Cook R.J., Wagner C. Dimethylglycine dehydrogenase and sarcosine dehydrogenase: mitochondrial folate-binding proteins from rat liver. Methods Enzymol. 122:1986;255-260
9. Lang H., Minaian K., Freudenberg N., Hoffmann R., Brandsch R. Tissue specificity of mitochondrial dimethylglycine dehydrogenase expression. Biochem. J. 299:1994;393-398
10. Porter D.H., Cook R.J., Wagner C. Enzymatic properties of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver. Arch. Biochem. Biophys. 243:1985;396-407
11. Mackenzie C.G., Frisell W.R. The metabolism of dimethylglycine by liver mitochondria. J. Biol. Chem. 232:1958;417-427
12. Hoskins D.D., Mackenzie C.G. Solubilization and electron transfer flavoprotein requirement of mitochondrial sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 236:1961;177-183
13. Frisell W.R., Mackenzie C.G. Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 237:1962;94-98
14. Frisell W.R., Mackenzie C.G. Sarcosine dehydrogenase and dimethylglycine dehydrogenase (Rat liver; Monkey liver). Methods Enzymol. A. 17:1970;976-981
15. Steenkamp D.J., Husain M. The effect of tetrahydrofolate on the reduction of electron transfer flavoprotein by sarcosine and dimethylglycine dehydrogenases. Biochem. J. 203:1982;707-715
16. Lang H., Polster M., Brandsch R. Rat liver dimethylglycine dehydrogenase. Flavinylation of the enzyme in hepatocytes in primary culture and characterisation of a cDNA clone. Eur. J. Biochem. 198:1991;793-799
17. Binzak B.A., Wevers R.A., Moolenaar S.H., Lee Y.M., Hwu W.L., Poggi-Bach J., Engelke U.F.H., Hoard H.M., Vockley J.G., Vockley J. Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency. Am. J. Hum. Genet. 68:2001;839-847
18. Moolenar S.H., Poggi-Bach J., Engelke U.F.H., Corstiaensen J.M.B., Heerschap A., deJong J.G.N., Binzak B.A., Vockley J., Wevers R.A. Defect in dimethylglycine dehydrogenase, a new inborn error of metabolism: NMR spectroscopy study. Clin. Chem. 45:1999;459-464
19. Chlumsky L.J., Zhang L., Jorns M.S. Sequence analysis of sarcosine oxidase genes reveals homologies with key enzymes of folate one-carbon metabolism. J. Biol. Chem. 270:1996;18252-18259
20. Leys D., Basran J., Scrutton N.S. Channelling and formation of "active" formaldehyde in dimethylglycine oxidase. EMBO J. 22:2003;4038-4048
21. Stoltz M., Rysavy P., Kalousek F., Brandsch R. Folding, flavinylation, and mitochondrial import of 6-hydroxy-D-nicotine oxidase fused to the presequence of rat dimethylglycine dehydrogenase. J. Biol. Chem. 270:1996;8016-8022
22. Cook R.J., Misono K.S., Wagner C. Identification of the covalently bound flavin of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver mitochondria. J. Biol. Chem. 259:1984;12475-12480
23. Cook R.J., Misono K.S., Wagner C. The amino acid sequences of the flavin-peptides of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver mitochondria. J. Biol. Chem. 260:1985;12998-13002
24. Otto A., Stoltz M., Sailer H.-P., Brandsch R. Biogenesis of the covalently flavinylated mitochondrial enzyme dimethylglycine dehydrogenase. J. Biol. Chem. 271:1996;9823-9829
25. Brizio C., Otto A., Brandsch R., Passarella S., Barile M. A protein factor of rat liver mitochondrial matrix involved in flavinylation of dimethylglycine dehydrogenase. Eur. J. Biochem. 267:2000;4346-4354
26. Brizio C., Barile M., Brandsch R. Flavinylation of the precursor of mitochondrial dimethylglycine dehydrogenase by intact and solubilised mitochondria. FEBS Lett. 522:2002;141-146
27. Berthold H., Scanarini M., Abney C.C., Frorath B., Northemann W. Purification of recombinant antigenic epitopes of the human 68-kDa (U1) ribonucleoprotein antigen using the expression system pH6EX3 followed by metal chelating affinity chromatography. Protein Expr. Purif. 3:1992;50-56
28. Waddel W.J., Hill C. A simple ultraviolet spectrophotometric method for determination of protein. J. Lab. Clin. Med. 48:1956;311-314
29. Bradford 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
30. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
31. Otto A., Stahle I., Klein R., Berg P.A., Pankuweit S., Brandsch R. Anti-mitochondrial antibodies in patients with dilated cardiomyopathy (anti-M7) are directed against flavoenzymes with covalently bound FAD. Clin. Exp. Immunol. 111:1998;541-547
32. Hefti M.H., Vervoort J., van Berkel W.J.H. Deflavination and reconstitution of flavoproteins. Tackling fold and function. Eur. J. Biochem. 270:2003;4227-4242