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Volumn 46, Issue 1, 2006, Pages 235-247

Enzymatic property analysis of p53R2 subunit of human ribonucleotide reductase

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; PROTEIN SUBUNIT; RIBONUCLEOTIDE REDUCTASE; RRM2B PROTEIN, HUMAN;

EID: 33748085352     PISSN: 00652571     EISSN: None     Source Type: Book Series    
DOI: 10.1016/j.advenzreg.2006.01.016     Document Type: Article
Times cited : (6)

References (29)
  • 1
    • 0037150125 scopus 로고    scopus 로고
    • EPR studies on a stable sulfinyl radical observed in the iron-oxygen-reconstituted Y177F/I263C protein R2 double mutant of ribonucleotide reductase from mouse
    • Adrait A., Ohrstrom M., Barra A.L., Thelander L., and Graslund A. EPR studies on a stable sulfinyl radical observed in the iron-oxygen-reconstituted Y177F/I263C protein R2 double mutant of ribonucleotide reductase from mouse. Biochem 41 (2002) 6510-6516
    • (2002) Biochem , vol.41 , pp. 6510-6516
    • Adrait, A.1    Ohrstrom, M.2    Barra, A.L.3    Thelander, L.4    Graslund, A.5
  • 2
    • 0026347398 scopus 로고
    • Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase
    • Bollinger Jr. J.M., Edmondson D.E., Huynh B.H., Filley J., Norton J.R., and Stubbe J. Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase. Science 253 (1991) 292-298
    • (1991) Science , vol.253 , pp. 292-298
    • Bollinger Jr., J.M.1    Edmondson, D.E.2    Huynh, B.H.3    Filley, J.4    Norton, J.R.5    Stubbe, J.6
  • 3
    • 0242317756 scopus 로고    scopus 로고
    • Mouse ribonucleotide reductase R2 protein: a new target for anaphase-promoting complex-Cdh1-mediated proteolysis
    • Chabes A., Pfleger C.M., Kirschner M.W., and Thelander L. Mouse ribonucleotide reductase R2 protein: a new target for anaphase-promoting complex-Cdh1-mediated proteolysis. Proc Natl Acad Sci USA 100 (2003) 3925-3929
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3925-3929
    • Chabes, A.1    Pfleger, C.M.2    Kirschner, M.W.3    Thelander, L.4
  • 4
    • 0037237032 scopus 로고    scopus 로고
    • Examination of the antiproliferative activity of iron chelators: multiple cellular targets and the different mechanism of action of triapine compared with desferrioxamine and the potent pyridoxal isonicotinoyl hydrazone analogue 311
    • Chaston T.B., Lovejoy D.B., Watts R.N., and Richardson D.R. Examination of the antiproliferative activity of iron chelators: multiple cellular targets and the different mechanism of action of triapine compared with desferrioxamine and the potent pyridoxal isonicotinoyl hydrazone analogue 311. Clin Cancer Res 9 (2003) 402-414
    • (2003) Clin Cancer Res , vol.9 , pp. 402-414
    • Chaston, T.B.1    Lovejoy, D.B.2    Watts, R.N.3    Richardson, D.R.4
  • 5
    • 0026652152 scopus 로고
    • Site-directed mutagenesis and deletion of the carboxyl terminus of escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction
    • Climent I., Sjoberg B.M., and Huang C.Y. Site-directed mutagenesis and deletion of the carboxyl terminus of escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction. Biochemistry 31 (1992) 4801-4807
    • (1992) Biochemistry , vol.31 , pp. 4801-4807
    • Climent, I.1    Sjoberg, B.M.2    Huang, C.Y.3
  • 7
    • 0032522647 scopus 로고    scopus 로고
    • The mammalian ribonucleotide reductase R2 component cooperates with a variety of oncogenes in mechanisms of cellular transformation
    • Fan H., Villegas C., Huang A., and Wright J.A. The mammalian ribonucleotide reductase R2 component cooperates with a variety of oncogenes in mechanisms of cellular transformation. Cancer Res 58 (1998) 1650-1653
    • (1998) Cancer Res , vol.58 , pp. 1650-1653
    • Fan, H.1    Villegas, C.2    Huang, A.3    Wright, J.A.4
  • 8
    • 0032832996 scopus 로고    scopus 로고
    • Triapine (3-aminopyridine-2-carboxaldehyde thiosemicarbazone; 3-AP): an inhibitor of ribonucleotide reductase with antineoplastic activity
    • Finch R.A., Liu M.C., Cory A.H., Cory J.G., and Sartorelli A.C. Triapine (3-aminopyridine-2-carboxaldehyde thiosemicarbazone; 3-AP): an inhibitor of ribonucleotide reductase with antineoplastic activity. Adv Enzyme Regul 39 (1999) 3-12
    • (1999) Adv Enzyme Regul , vol.39 , pp. 3-12
    • Finch, R.A.1    Liu, M.C.2    Cory, A.H.3    Cory, J.G.4    Sartorelli, A.C.5
  • 9
    • 0035798630 scopus 로고    scopus 로고
    • 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
    • Guittet O., Hakansson P., Voevodskaya N., Fridd S., Graslund A., Arakawa H., 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 276 (2001) 40647-40651
    • (2001) J Biol Chem , vol.276 , pp. 40647-40651
    • Guittet, O.1    Hakansson, P.2    Voevodskaya, N.3    Fridd, S.4    Graslund, A.5    Arakawa, H.6
  • 10
    • 0028078272 scopus 로고
    • The stable tyrosyl radical in mouse ribonucleotide reductase is not essential for enzymatic activity
    • Henriksen M.A., Cooperman B.S., Salem J.S., Li L.-S., and Rubin H. The stable tyrosyl radical in mouse ribonucleotide reductase is not essential for enzymatic activity. J Am Chem Soc 116 (1994) 9773-9774
    • (1994) J Am Chem Soc , vol.116 , pp. 9773-9774
    • Henriksen, M.A.1    Cooperman, B.S.2    Salem, J.S.3    Li, L.-S.4    Rubin, H.5
  • 11
  • 12
    • 0030580112 scopus 로고    scopus 로고
    • The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than escherichia coli R2
    • Kauppi B., Nielsen B.B., Ramaswamy S., Larsen I.K., Thelander M., Thelander L., 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 262 (1996) 706-720
    • (1996) J Mol Biol , vol.262 , pp. 706-720
    • Kauppi, B.1    Nielsen, B.B.2    Ramaswamy, S.3    Larsen, I.K.4    Thelander, M.5    Thelander, L.6
  • 13
    • 0042166135 scopus 로고    scopus 로고
    • Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools
    • (Epub ahead of print on PubMed)
    • Kimura T., Takeda S., Sagiya Y., Gotoh M., Nakamura Y., and Arakawa H. Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools. Nat Genet (2003) (Epub ahead of print on PubMed)
    • (2003) Nat Genet
    • Kimura, T.1    Takeda, S.2    Sagiya, Y.3    Gotoh, M.4    Nakamura, Y.5    Arakawa, H.6
  • 14
    • 0034594895 scopus 로고    scopus 로고
    • p53 sends nucleotides to repair DNA
    • Lozano G., and Elledge S.J. p53 sends nucleotides to repair DNA. Nature 404 (2000) 24-25
    • (2000) Nature , vol.404 , pp. 24-25
    • Lozano, G.1    Elledge, S.J.2
  • 15
    • 0025829053 scopus 로고
    • Purification and characterization of recombinant mouse and herpes simplex virus ribonucleotide reductase R2 subunit
    • Mann G.J., Graslund A., Ochiai E., Ingemarson R., and Thelander L. Purification and characterization of recombinant mouse and herpes simplex virus ribonucleotide reductase R2 subunit. Biochem 30 (1991) 1939-1947
    • (1991) Biochem , vol.30 , pp. 1939-1947
    • Mann, G.J.1    Graslund, A.2    Ochiai, E.3    Ingemarson, R.4    Thelander, L.5
  • 16
    • 0034738967 scopus 로고    scopus 로고
    • A ribonucleotide reductase gene is a transcriptional target of p53 and p73
    • Nakano K., Balint E., Ashcroft M., and Vousden K.H. A ribonucleotide reductase gene is a transcriptional target of p53 and p73. Oncogene 19 (2000) 4283-4289
    • (2000) Oncogene , vol.19 , pp. 4283-4289
    • Nakano, K.1    Balint, E.2    Ashcroft, M.3    Vousden, K.H.4
  • 17
    • 0027521831 scopus 로고
    • Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators
    • Nyholm S., Mann G.J., Johansson A.G., Bergeron R.J., Graslund A., and Thelander L. Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators. J Biol Chem 268 (1993) 26200-26205
    • (1993) J Biol Chem , vol.268 , pp. 26200-26205
    • Nyholm, S.1    Mann, G.J.2    Johansson, A.G.3    Bergeron, R.J.4    Graslund, A.5    Thelander, L.6
  • 18
    • 0037122708 scopus 로고    scopus 로고
    • Synthesis, biological evaluation, and quantitative structure-activity relationship analysis of new Schiff bases of hydroxysemicarbazide as potential antitumor agents
    • Ren S., Wang R., Komatsu K., Bonaz-Krause P., Zyrianov Y., McKenna C.E., et al. Synthesis, biological evaluation, and quantitative structure-activity relationship analysis of new Schiff bases of hydroxysemicarbazide as potential antitumor agents. J Med Chem 45 (2002) 410-419
    • (2002) J Med Chem , vol.45 , pp. 410-419
    • Ren, S.1    Wang, R.2    Komatsu, K.3    Bonaz-Krause, P.4    Zyrianov, Y.5    McKenna, C.E.6
  • 19
    • 0036269005 scopus 로고    scopus 로고
    • Iron chelators as therapeutic agents for the treatment of cancer
    • Richardson D.R. Iron chelators as therapeutic agents for the treatment of cancer. Crit Rev Oncol Hematol 42 (2002) 267-281
    • (2002) Crit Rev Oncol Hematol , vol.42 , pp. 267-281
    • Richardson, D.R.1
  • 20
    • 0033588374 scopus 로고    scopus 로고
    • Evidence by mutagenesis that Tyr370 of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathway
    • Rova U., Adrait A., Potsch S., Graslund A., and Thelander L. Evidence by mutagenesis that Tyr370 of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathway. J Biol Chem 274 (1999) 23746-23751
    • (1999) J Biol Chem , vol.274 , pp. 23746-23751
    • Rova, U.1    Adrait, A.2    Potsch, S.3    Graslund, A.4    Thelander, L.5
  • 21
    • 0028234539 scopus 로고
    • Tryptophan radicals formed by iron/oxygen reaction with Escherichia coli ribonucleotide reductase protein R2 mutant Y122F
    • Sahlin M., Lassmann G., Potsch S., Slaby A., Sjoberg B.M., and Graslund A. Tryptophan radicals formed by iron/oxygen reaction with Escherichia coli ribonucleotide reductase protein R2 mutant Y122F. J Biol Chem 269 (1994) 11699-11702
    • (1994) J Biol Chem , vol.269 , pp. 11699-11702
    • Sahlin, M.1    Lassmann, G.2    Potsch, S.3    Slaby, A.4    Sjoberg, B.M.5    Graslund, A.6
  • 22
    • 1642453838 scopus 로고    scopus 로고
    • In vitro characterization of enzyme properties and inhibition of the p53R2 subunit of human ribonucleotide reductase
    • Shao J., Zhou B., Zhu L., Qiu W., Yuan Y., Xi B., and Yen Y. In vitro characterization of enzyme properties and inhibition of the p53R2 subunit of human ribonucleotide reductase. Cancer Res 64 (2004) 1-6
    • (2004) Cancer Res , vol.64 , pp. 1-6
    • Shao, J.1    Zhou, B.2    Zhu, L.3    Qiu, W.4    Yuan, Y.5    Xi, B.6    Yen, Y.7
  • 24
    • 0037374051 scopus 로고    scopus 로고
    • Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits
    • Xue L., Zhou B., Liu X., Qiu W., Jin Z., and Yen Y. Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res 63 (2003) 980-986
    • (2003) Cancer Res , vol.63 , pp. 980-986
    • Xue, L.1    Zhou, B.2    Liu, X.3    Qiu, W.4    Jin, Z.5    Yen, Y.6
  • 26
    • 0028107848 scopus 로고
    • Characterization of a hydroxyurea-resistant human KB cell line with supersensitivity to 6-thioguanine
    • Yen Y., Grill S.P., Dutschman G.E., Chang C.N., Zhou B.S., and Cheng Y.C. Characterization of a hydroxyurea-resistant human KB cell line with supersensitivity to 6-thioguanine. Cancer Res 54 (1994) 3686-3691
    • (1994) Cancer Res , vol.54 , pp. 3686-3691
    • Yen, Y.1    Grill, S.P.2    Dutschman, G.E.3    Chang, C.N.4    Zhou, B.S.5    Cheng, Y.C.6
  • 27
    • 0028928261 scopus 로고
    • Overexpression of ribonucleotide reductase in transfected human KB cells increases their resistance to hydroxyurea: M2 but not M1 is sufficient to increase resistance to hydroxyurea in transfected cells
    • Zhou B.S., Hsu N.Y., Pan B.C., Doroshow J.H., and Yen Y. Overexpression of ribonucleotide reductase in transfected human KB cells increases their resistance to hydroxyurea: M2 but not M1 is sufficient to increase resistance to hydroxyurea in transfected cells. Cancer Res 55 (1995) 1328-1333
    • (1995) Cancer Res , vol.55 , pp. 1328-1333
    • Zhou, B.S.1    Hsu, N.Y.2    Pan, B.C.3    Doroshow, J.H.4    Yen, Y.5
  • 28
    • 0142250911 scopus 로고    scopus 로고
    • The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53
    • Zhou B., Liu X., Mo X., Xue L., Darwish D., Qiu W., Shih J., Hwu E.B., Luh F., and Yen Y. The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53. Cancer Res 63 (2003) 6583-6594
    • (2003) Cancer Res , vol.63 , pp. 6583-6594
    • Zhou, B.1    Liu, X.2    Mo, X.3    Xue, L.4    Darwish, D.5    Qiu, W.6    Shih, J.7    Hwu, E.B.8    Luh, F.9    Yen, Y.10
  • 29
    • 0031938457 scopus 로고
    • Overexpression of transfected human ribonucleotide reductase M2 subunit in human cancer cells enhances their invasive potential
    • Zhou B.S., Tsai P., Ker R., Tsai J., Ho R., Yu J., Shih J., and Yen Y. Overexpression of transfected human ribonucleotide reductase M2 subunit in human cancer cells enhances their invasive potential. Clin Exp Metastasis 16 (1995) 43-49
    • (1995) Clin Exp Metastasis , vol.16 , pp. 43-49
    • Zhou, B.S.1    Tsai, P.2    Ker, R.3    Tsai, J.4    Ho, R.5    Yu, J.6    Shih, J.7    Yen, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.