RNA with iron(II) as a cofactor catalyses electron transfer

Nature Chemistry

Volumn 5, Issue 6, 2013, Pages 525-528

  Hsiao, Chiaolong ^a   Chou, I Chun ^a   Okafor, C Denise ^a   Bowman, Jessica C ^a   O'neill, Eric B ^a   Athavale, Shreyas S ^a   Petrov, Anton S ^a   Hud, Nicholas V ^a   Wartell, Roger M ^a   Harvey, Stephen C ^a   Williams, Loren Dean ^a  

^a GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IRON; RNA;

ARTICLE; BIOCATALYSIS; ELECTRON TRANSPORT; METABOLISM;

BIOCATALYSIS; ELECTRON TRANSPORT; IRON; RNA;

MLCS; MLOWN;

EID: 84879075676     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.1649     Document Type: Article

References (33)

1. Anbar, A. D. Oceans. Elements and evolution. Science 322, 1481-1483 (2008).
2. Hazen, R. M. & Ferry, J. M. Mineral evolution: mineralogy in the fourth dimension. Elements 6, 9-12 (2010).
3. Prousek, J. Fenton chemistry in biology and medicine. Pure Appl. Chem. 79, 2325-2338 (2007).
4. Klein, C. Some Precambrian banded iron-formations (BIFs) from around the world: their age, geologic setting, mineralogy, metamorphism, geochemistry, and origin. Am. Mineral. 90, 1473-1499 (2005).
5. Aguirre, J. D. & Culotta, V. C. Battles with iron: manganese in oxidative stress protection. J. Biol. Chem. 287, 13541-13548 (2012).
6. Ushizaka, S., Kuma, K. & Suzuki, K. Effects of Mn and Fe on growth of a coastal marine diatom Thalassiosira weissflogii in the presence of precipitated Fe(III) hydroxide and EDTA-Fe(III) complex. Fish. Sci. 77, 411-424 (2011).
7. Martin, J. E. & Imlay, J. A. The alternative aerobic ribonucleotide reductase of Escherichia coli, NrdEF, is a manganese-dependent enzyme that enables cell replication during periods of iron starvation. Mol. Microbiol. 80, 319-334 (2011).
8. Cotruvo, J. A. & Stubbe, J. Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo. Annu. Rev. Biochem. 80, 733-767 (2011).
9. Anjem, A., Varghese, S. & Imlay, J. A. Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol. Microbiol. 72, 844-858 (2009).
10. Wolfe-Simon, F., Starovoytov, V., Reinfelder, J. R., Schofield, O. & Falkowski, P. G. Localization and role of manganese superoxide dismutase in a marine diatom. Plant Physiol. 142, 1701-1709 (2006).
11. Jordan, A. & Reichard, P. Ribonucleotide reductases. Annu. Rev. Biochem. 67, 71-98 (1998).
12. Athavale, S. S. et al. RNA folding and catalysis mediated by iron(II). PLoS ONE 7, e38024 (2012).
13. Fox, G. E. Origin and evolution of the ribosome. Cold Spring Harb. Perspect. Biol. 2, a003483 (2010).
14. Bowman, J. C., Lenz, T. K., Hud, N. V. & Williams, L. D. Cations in charge: magnesium ions in RNA folding and catalysis. Curr. Opin. Struct. Biol. 22, 262-272 (2012).
15. Auffinger, P., Grover, N. & Westhof, E. Metal ion binding to RNA. Met. Ions Life Sci. 9, 1-35 (2011).
16. Brion, P. & Westhof, E. Hierarchy and dynamics of RNA folding. Annu. Rev. Biophys. Biomol. Struct. 26, 113-137 (1997).
17. Stein, A. & Crothers, D. M. Conformational changes of transfer RNA. The role of magnesium(II). Biochemistry 15, 160-168 (1976).
18. Lynch, D. C. & Schimmel, P. R. Cooperative binding of magnesium to transfer ribonucleic acid studied by a fluorescent probe. Biochemistry 13, 1841-1852 (1974).
19. Lindahl, T., Adams, A. & Fresco, J. R. Renaturation of transfer ribonucleic acids through site binding of magnesium. Proc. Natl Acad. Sci. USA 55, 941-948 (1966).
20. Petrov, A. et al. RNA-magnesium-protein interactions in large ribosomal subunit. J. Phys. Chem. B 116, 8113-8120 (2012).
21. Butcher, S. E. The spliceosome and its metal ions. Met. Ions Life Sci. 9, 235-251 (2011).
22. Johnson-Buck, A. E., McDowell, S. E. & Walter, N. G. Metal ions: supporting actors in the playbook of small ribozymes. Met. Ions Life Sci. 9, 175-196 (2011).
23. Josephy, P. D., Eling, T. & Mason, R. P. The horseradish peroxidase-catalyzed oxidation of 3,5,3′,5′-tetramethylbenzidine. Free radical and charge-transfer complex intermediates. J. Biol. Chem. 257, 3669-3675 (1982).
24. Larson, S. B., Day, J., Greenwood, A. & McPherson, A. Refined structure of satellite tobacco mosaic virus at 1.8 Å resolution. J. Mol. Biol. 277, 37-59 (1998).
25. Hsiao, C. & Williams, L. D. A recurrent magnesium-binding motif provides a framework for the ribosomal peptidyl transferase center. Nucleic Acids Res. 37, 3134-3142 (2009).
26. Klein, D. J., Moore, P. B. & Steitz, T. A. The contribution of metal ions to the structural stability of the large ribosomal subunit. RNA 10, 1366-1379 (2004).
27. Cate, J. H., Hanna, R. L. & Doudna, J. A. A magnesium ion core at the heart of a ribozyme domain. Nature Struct. Biol. 4, 553-558 (1997).
28. Berens, C., Streicher, B., Schroeder, R. & Hillen, W. Visualizing metal-ionbinding sites in group I introns by iron(II)-mediated Fenton reactions. Chem. Biol. 5, 163-175 (1998).
29. Zivarts, M., Liu, Y. & Breaker, R. R. Engineered allosteric ribozymes that respond to specific divalent metal ions. Nucleic Acids Res. 33, 622-631 (2005).
30. 2+ binds iron responsive element-RNA, selectively changing protein-binding affinities and regulating mRNA repression and activation. Proc. Natl Acad. Sci. USA 109, 8417-8422 (2012).
31. Honda, K. et al. Ribosomal RNA in Alzheimer disease is oxidized by bound redox-active iron. J. Biol. Chem. 280, 20978-20986 (2005).
32. 2+-dependent redox active ribozyme. J. Am. Chem. Soc. 126, 5044-5045 (2004).
33. Sen, D. & Poon, L. C. RNA and DNA complexes with hemin [Fe(III) heme] are efficient peroxidases and peroxygenases: how do they do it and what does it mean? Crit. Rev. Biochem. Mol. Biol. 46, 478-492 (2011).