Structure-function roles of four cysteine residues in the human arsenic (+3 oxidation state) methyltransferase (hAS3MT) by site-directed mutagenesis

Chemico-Biological Interactions

Volumn 179, Issue 2-3, 2009, Pages 321-328

  Song, Xiaoli ^a   Geng, Zhirong ^a   Zhu, Jingshu ^a   Li, Chengying ^a   Hu, Xin ^b   Bian, Ningsheng ^a   Zhang, Xinrong ^c   Wang, Zhilin ^a  

^a NANJING UNIVERSITY   (China)

^b NANJING UNIVERSITY   (China)

^c BEIJING UNIVERSITY OF POSTS AND TELECOMMUNICATIONS   (China)

Author keywords

Activity cites; Arsenic; Cysteine residues; Human arsenic methyltransferase; Site directed mutagenesis; Structure function roles

Indexed keywords

ARSENIC DERIVATIVE; CYSTEINE; SELENIUM; SERINE; THIOL;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HUMAN; INFRARED SPECTROSCOPY; METHYLATION; POLYMERASE CHAIN REACTION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ARSENIC; CIRCULAR DICHROISM; CYSTEINE; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; KINETICS; METHYLATION; METHYLTRANSFERASES; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY; SELENIUM; SERINE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; STRUCTURE-ACTIVITY RELATIONSHIP;

RATTUS;

EID: 62549098120     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.12.018     Document Type: Article

References (42)

1. National Research Council. Essentiality and Therapeutic Uses, Arsenic in Drinking Water (1999), National Academy Press, Washington, DC pp. 251-263
2. Xu Y.Y., Wang Y., Zheng Q.M., Li B., Li X., Jin Y.P., Lv X.Q., Qu G., and Sun G.F. Clinical manifestations and arsenic methylation after a rare subacute arsenic poisoning accident. Toxicol. Sci. 103 (2008) 278-284
3. Cullen W.R., McBride B.C., and Reglinski J. The reduction of trimethylarsine oxide to trimethylarsine by thiols: a mechanistic model for the biological reduction of arsenicals. J. Inorg. Biochem. 21 (1984) 45-60
4. Aposhian H.V. Enzymatic methylation of arsenic species and other new approaches to arsenic toxicity. Annu. Rev. Pharmacol. Toxicol. 37 (1997) 397-419
5. Hayakawa T., Kobayashi Y., Cui X., and Hirano S. A new metabolic pathway of arsenite: arsenic-glutathione complexes are substrates for human arsenic methyltransferase Cyt19. Arch. Toxicol. 79 (2005) 183-191
6. Gebel T.W. Arsenic methylation is a process of detoxification through accelerated excretion. Int. J. Hyg. Environ. Health 205 (2002) 505-508
7. Nesnow S., Roop B.C., Lambert G., Kadiiska M., Mason R.P., Cullen W.R., and Mass M.J. DNA damage induced by methylated trivalent arsenicals is mediated by reactive oxygen species. Chem. Res. Toxicol. 12 (2002) 1627-1634
8. Styblo M., DelRazo L.M., Vega L., Germolec D.R., LeCluyse E.L., Hamilton G.A., Reed W., Wang C.Q., Cullen W.R., and Thomas D.J. Comparative toxicity of trivalent and pentavalent inorganic and methylated arsenicals in rat and human cells. Arch. Toxicol. 74 (2000) 289-299
9. Thomas D.J., Styblo M., and Lin S. The cellular metabolism and systemic toxicity of arsenic. Toxicol. Appl. Pharmacol. 176 (2001) 127-144
10. Mass M.J., Tennant A., Roop B.C., Cullen W.R., Styblo M., Thomas D.J., and Kligerman A.D. Methylated trivalent arsenic species are genotoxic. Chem. Res. Toxicol. 14 (2001) 355-361
11. Schwerdtle T., Walter I., Mackiw I., and Hartwig A. Induction of oxidative DNA damage by arsenite and its trivalent and pentavalent methylated metabolites in cultured human cells and isolated DNA. Carcinogenesis 24 (2003) 967-974
12. Vahter M. Genetic polymorphism in the biotransformation of inorganic arsenic and its role in toxicity. Toxicol. Lett. 112-113 (2000) 209-217
13. Chung J.S., Kalman D.A., Moore L.E., Kosnett M.J., Arroyo A.P., Beeris M., Mazumder D.N., Hernandez A.L., and Smith A.H. Family correlations of arsenic methylation patterns in children and parents exposed to high concentrations of arsenic in drinking water. Environ. Health Perspect. 110 (2002) 729-733
14. Mukhopadhyay R., and Rosen B.P. Arsenate reductases in prokaryotes and eukaryotes. Environ. Health Perspect. 110 Suppl. 5 (2002) 745-748
15. Fomenko D.E., Xing W.B., Adair B.M., Thomas D.J., and Gladyshev V.N. High-throughput identification of catalytic redox-active cysteine residues. Science 315 (2007) 387-389
16. Li J.X., Waters S.B., Drobna Z., Devesa V., Styblob M., and Thomas D.J. Arsenic (+3 oxidation state) methyltransferase and the inorganic arsenic methylation phenotype. Toxicol. Appl. Pharmacol. 204 (2005) 164-169
17. Beeby M., O'Connor B.D., Ryttersgaard C., Boutz D.R., and Perry L.J. The Genomics of disulfide bonding and protein stabilization in thermophiles. PLoS Biol. 3 (2005) 1549-1558
18. Z.R. Geng, X.L. Song, Z. Xing, J.L. Geng, S.C. Zhang, X.R. Zhang, Z.L. Wang, Effects of selenium on the structure and function of recombinant human S-adenosyl-l-methionine dependent arsenic (III) methyltransferase in E. coli, J. Biol. Inorg. Chem., doi:10.1007/s00775-008-0464-6.
19. Sanger F., Nicklen S., and Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. U.S.A. 7 (1977) 5463-5467
20. III-methyltransferase and the methylation of arsenite by rat and human hepatocytes. Chem. Res. Toxicol. 16 (2003) 261-265
21. Yang Y.T., Wu C.S.C., and Martinez H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130 (1986) 208-257
22. Ellman G.L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82 (1959) 70-77
23. Lin S., Shi Q., Nix F.B., Styblo M., Beck M.A., Herbin-Davis K.M., Hall L.L., Simeonsson J.B., and Thomas D.J. A novel S-adenosyl-l-methionine: arsenic(III) methyltransferase from rat liver cytosol. J. Biol. Chem. 277 (2002) 10795-10803
24. Vahter M. Species differences in the metabolism of arsenic compounds. Appl. Organomet. Chem. 8 (1994) 175-182
25. Zakharyan R.A., Wildfang E., and Aposhian H.V. Enzymatic methylation of arsenic compounds. III. The marmoset and tamarin, but not the rhesus monkey, are deficient in methyltransferase that methylate inorganic arsenic. Toxicol. Appl. Pharmacol. 140 (1996) 77-84
26. Healy S.M., Zakharyan R.A., and Aposhian H.V. Enzymatic methylation of arsenic compounds. IV. In vitro and in vivo deficiency of the methylation of arsenite and monomethylarsonic acid in the guinea pig. Mutat. Res. 386 (1997) 229-239
27. Aposhian H.V., Zakharyan R.A., Avram M.D., Sampayo-Reyes A., and Wollenberg M.L. A review of the enzymology of arsenic metabolism and a new potential role of hydrogen peroxide in the detoxication of the trivalent arsenic species. Toxicol. Appl. Pharmacol. 198 (2004) 327-335
28. Kedderis G.L., Elmore A.R., Crecelius E.A., Yager J.W., and Goldsworthy T.L. Kinetics of arsenic methylation by freshly isolated B6C3F1 mouse hepatocytes. Chem. Biol. Interact. 16 (2006) 139-145
29. Cleland W.W. Steady state kinetics. In: Boyer P.D. (Ed). The Enzymes vol. 2 (1970), Academic Press, New York 1-65
30. Levander O.A. Metabolic interrelationships between arsenic and selenium. Environ. Health Perspect. 19 (1977) 159-164
31. Styblo M., and Thomas D.J. Selenium modifies the metabolism and toxicity of arsenic in primary rat hepatocytes. Toxicol. Appl. Pharmacol. 172 (2001) 52-61
32. Sarver R.W.J., and Krueger W.C. An infrared and circular dichroism combined approach to the analysis of protein secondary structure. Anal. Biochem. 199 (1991) 61-67
33. Yang J.T., Wu C.S.C., and Martinez H.M. Calculation of protein conformation from circular-dichroism. Methods Enzymol. 130 (1986) 208-269
34. Hennessey J.P., and Johnson W.C. Information-content in the circular-dichroism of proteins. Biochemistry 20 (1981) 1085-1094
35. Levitt M., and Chothia C. Structural patterns in globular proteins. Nature 261 (1976) 552-558
36. Krimm S., and Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 38 (1986) 181-364
37. Surewicz W.K., and Mantsch H.H. New insight into protein secondary structure from resolution-enhanced infrared-spectra. Biochim. Biophys. Acta 952 (1988) 115-130
38. Dong A., Huang P., and Caughey W.S. Redox-dependent changes in beta-extended chain and turn structures of cytochrome-c in water solution determined by 2nd derivative amide-I infrared-spectra. Biochemistry 31 (1992) 182-189
39. Sun W.Y., Fang J.L., Cheng M., Xia P.Y., and Tang W.X. Secondary structure dependent on metal ions of copper, zinc superoxide dismutase investigated by Fourier transform IR spectroscopy. Biopolymers 42 (1997) 297-303
40. Ghosh K.J., Peisajovich S.G., and Shai Y. Sendai virus internal fusion peptide: structural and functional characterization and a plausible mode of viral entry inhibition. Biochemistry 39 (2000) 11581-11592
41. Byler D.M., Brouillette J.N., and Susi H. Quantitative studies of protein structure by FTIR spectral deconvolution and curve fitting. Spectroscopy 3 (1986) 29-32
42. Dong A.C., and Caughey W.S. Infrared methods for study of hemoglobin reactions and structures. Methods Enzymol. 232 (1994) 139-175