A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases

Molecular Cancer Therapeutics

Volumn 4, Issue 12, 2005, Pages 1830-1836

  Zhou, Bingsen ^a   Shao, Jimin ^a,b   Su, Leila ^a   Yuan, Yate Ching ^a   Qi, Christina ^a   Shih, Jennifer ^a   Xi, Bixin ^a   Chu, Bernard ^a   Yen, Yun ^a  

^a CITY OF HOPE NATIONAL MEDICAL CENTER   (United States)

^b ZHEJIANG UNIVERSITY SCHOOL OF MEDICINE   (China)

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEOTIDE; PLASMID DNA; PROTEIN P53; RIBONUCLEOTIDE REDUCTASE; TYROSINE; TYROSINE DERIVATIVE;

ARTICLE; CATALYSIS; CHLAMYDIA; DNA SYNTHESIS; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME ASSAY; ESCHERICHIA COLI; GENE CLUSTER; GENE MUTATION; GENETIC ANALYSIS; GENETIC CODE; HUMAN; IN VITRO STUDY; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING; YEAST;

AMINO ACID SEQUENCE; BASE SEQUENCE; CATALYSIS; DNA PRIMERS; ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; IRON; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RIBONUCLEOTIDE REDUCTASES; SPECTROPHOTOMETRY, ATOMIC; TYROSINE;

EID: 30344471090     PISSN: 15357163     EISSN: None     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-05-0273     Document Type: Article

References (26)

1. Reichard P. From RNA to DNA, why so many ribonucleotide reductases? Science 1993;260:1773-7.
2. Stubbe J. Di-iron-tyrosyl radical ribonucleotide reductases. Curr Opin Chem Biol 2003;7:183-8.
3. Tanaka H, Arakawa H, Yamaguchi T, et al. A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage. Nature 2000;404:42-9.
4. Guittet O, Hakansson P, Voevodskaya N, et al. Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells. J Biol Chem 2001;276:40647-51.
5. Xue L, Zhou B, Liu X, et al. Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res 2003;63:980-6.
6. Shao J, Zhou B, Zhu L, et al. In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase. Cancer Res 2004;64:1-6.
7. Nordlund P, Sjoberg BM, Eklund H. Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature 1990;345:593-8.
8. Thelander L, Graslund A, Thelander M. Continual presence of oxygen and iron required for mammalian ribonucleotide reduction: possible regulation mechanism. Biochem Biophys Res Commun 1983;110:859-65.
9. Strand KR, Karlsen S, Kolberg M, et al. Crystal structural studies of changes in the native dinuclear iron center of ribonucleotide reductase protein R2 from mouse. J Biol Chem 2004;279:46794-801.
10. Schmidt PP, Andersson KK, Barra AL, et al. High field EPR studies of mouse ribonucleotide reductase indicate hydrogen bonding of the tyrosyl radical. J Biol Chem 1996;271:23615-8.
11. Kauppi B, Nielsen BE, Ramaswamy S, et al. The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. J Mol Biol 1996;262:706-20.
12. Nyholm S, Mann GJ, Johansson AG, et al. Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators. J Biol Chem 1993;268:26200-5.
13. Sahlin M, Petersson L, Graslund A, et al. Magnetic interaction between the tyrosyl free radical and the antiferromagnetically coupled iron center in ribonucleotide reductase. Biochemistry 1987;26:5541-8.
14. Davydov RM, Davydov A, Ingemarson R, et al. EPR study of the mixed-valent diiron sites in mouse and herpes simplex virus ribonucleotide reductases. Effect of the tyrosyl radical on structure and reactivity of the diferric center. Biochemistry 1997;36:9093-100.
15. Hogbom M, Stenmark P, Voevodskaya N, et al. The radical site in chlamydial ribonucleotide reductase defines a new R2 subclass. Science 2004;305:245-8.
16. Sahlin M, Lassmann G, Potsch S, et al. Tryptophan radicals formed by iron/oxygen reaction with Escherichia coli ribonucleotide reductase protein R2 mutant Y122F. J Biol Chem 1994;269:11699-702.
17. Shao J, Zhou B, Zhu L, et al. Determination of the potency and subunit-selectivity of ribonucleotide reductase inhibitors with a recombinant-holoenzyme-based in vitro assay. Biochem Pharmacol 2005;69: 627-34.
18. Pesavento RP, van der Donk WA. Tyrosyl radical cofactors. Adv Protein Chem 2001;58:317-85.
19. Henriksen MA, Cooperman BS, Salem JS, et al. The stable tyrosyl radical in mouse ribonucleotide reductase is not essential for enzymatic activity. J Am Chem Soc 1994;116:9773-4.
20. Bollinger JM, Jr., Edmondson DE, Huynh BH, et al. Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase. Science 1991;253:292-8.
21. Potsch S, Lendzian F, Ingemarson R, et al. The iron-oxygen reconstitution reaction in protein R2-Tyr-177 mutants of mouse ribonucleotide reductase. EPR and electron nuclear double resonance studies on a new transient tryptophan radical. J Biol Chem 1999;274: 17696-704.
22. Climent I, Sjoberg BM, Huang CY. Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction. Biochemistry 1992;31:4801-7.
23. Rova U, Adrait A, Potsch S, et al. Evidence by mutagenesis that Tyr(370) of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathway. J Biol Chem 1999;274:23746-51.
24. Svistunenko DA, Cooper CE. A new method of identifying the site of tyrosyl radicals in proteins. Biophys J 2004;87:582-95.
25. Katterle B, Sahlin M, Schmidt PP, et al. Kinetics of transient radicals in Escherichia coli ribonucleotide reductase. Formation of a new tyrosyl radical in mutant protein R2. J Biol Chem 1997;272:10414-21.
26. Larsson A, Sjoberg BM. Identification of the stable free radical tyrosine residue in ribonucleotide reductase. EMBO J 1986;5:2037-40.