메뉴 건너뛰기




Volumn 19, Issue 16, 2005, Pages 1920-1933

Control of dTTP pool size by anaphase promoting complex/cyclosome is essential for the maintenance of genetic stability

Author keywords

APC C; Cell cycle; dNTP pool imbalance; dTTP; Genome stability

Indexed keywords

ANAPHASE PROMOTING COMPLEX; THYMIDINE TRIPHOSPHATE;

EID: 23944450180     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1322905     Document Type: Article
Times cited : (75)

References (41)
  • 2
    • 0023487248 scopus 로고
    • Regulation of pyrimidine deoxyribonucleotide metabolism by substrate cycles in dCMP deaminase-deficient V79 hamster cells
    • Bianchi, V., Pontis, E., and Reichard, P. 1987. Regulation of pyrimidine deoxyribonucleotide metabolism by substrate cycles in dCMP deaminase-deficient V79 hamster cells. Mol. Cell. Biol. 7: 4218-4224.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 4218-4224
    • Bianchi, V.1    Pontis, E.2    Reichard, P.3
  • 3
    • 0015919830 scopus 로고
    • Effects of thymidine on deoxyribonucleoside triphosphate pools and deoxyribonucleic acid synthesis in Chinese hamster ovary cells
    • Bjursell, G. and Reichard, P. 1973. Effects of thymidine on deoxyribonucleoside triphosphate pools and deoxyribonucleic acid synthesis in Chinese hamster ovary cells. J. Biol. Chem. 248: 3904-3909.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3904-3909
    • Bjursell, G.1    Reichard, P.2
  • 4
    • 9744284973 scopus 로고    scopus 로고
    • ATM is required for the cellular response to thymidine induced replication fork stress
    • Bolderson, E., Scorah, J., Helleday, T., Smythe, C., and Meuth, M. 2004. ATM is required for the cellular response to thymidine induced replication fork stress. Hum. Mol. Genet. 13: 2937-2945.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2937-2945
    • Bolderson, E.1    Scorah, J.2    Helleday, T.3    Smythe, C.4    Meuth, M.5
  • 5
    • 0020822951 scopus 로고
    • Molecular cloning and cell cycle-specific regulation of a functional human thymidine kinase gene
    • Bradshaw Jr., H.D. 1983. Molecular cloning and cell cycle-specific regulation of a functional human thymidine kinase gene. Proc. Natl. Acad. Sci. 80: 5588-5591.
    • (1983) Proc. Natl. Acad. Sci. , vol.80 , pp. 5588-5591
    • Bradshaw Jr., H.D.1
  • 6
    • 0029789637 scopus 로고    scopus 로고
    • The proteolysis of mitotic cyclins in mammalian cells persists from the end of mitosis until the onset of S phase
    • Brandeis, M. and Hunt, T. 1996. The proteolysis of mitotic cyclins in mammalian cells persists from the end of mitosis until the onset of S phase. EMBO J. 15: 5280-5289.
    • (1996) EMBO J. , vol.15 , pp. 5280-5289
    • Brandeis, M.1    Hunt, T.2
  • 7
    • 0242317756 scopus 로고    scopus 로고
    • Mouse ribonuclotide reductase R2 protein: A new target for anaphase-promoting complex-Cdh1-mediated proteolysis
    • Chabes, A.L., Pfleger, C.M., Kirschner, M.W., and Thelander, L. 2003a. Mouse ribonuclotide reductase R2 protein: A new target for anaphase-promoting complex-Cdh1-mediated proteolysis. Proc. Natl. Acad. Sci. 100: 3925-3929.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 3925-3929
    • Chabes, A.L.1    Pfleger, C.M.2    Kirschner, M.W.3    Thelander, L.4
  • 8
    • 0037423223 scopus 로고    scopus 로고
    • Survival of DNA damage in yeast directly depends on increased dNTP levels allowed by related feedback inhibition of ribonucleotide reductase
    • Chabes, A., Georgieva, B., Domkin, V., Zhao, X., Rothstein, R., and Thelander, L. 2003b. Survival of DNA damage in yeast directly depends on increased dNTP levels allowed by related feedback inhibition of ribonucleotide reductase. Cell 112: 391-401.
    • (2003) Cell , vol.112 , pp. 391-401
    • Chabes, A.1    Georgieva, B.2    Domkin, V.3    Zhao, X.4    Rothstein, R.5    Thelander, L.6
  • 9
    • 0028087601 scopus 로고
    • Differential phosphorylation of human thymidine kinase in proliferating and M phase-arrested human cells
    • Chang, Z.F., Huang, D.Y., and Hsue, N.C. 1994. Differential phosphorylation of human thymidine kinase in proliferating and M phase-arrested human cells. J. Biol. Chem. 269: 21249-21254.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21249-21254
    • Chang, Z.F.1    Huang, D.Y.2    Hsue, N.C.3
  • 10
    • 0032524346 scopus 로고    scopus 로고
    • Serine 13 is the site of mitotic phosphorylation of human thymidine kinase
    • Chang, Z.F., Huang, D.Y., and Chi, L.M. 1998. Serine 13 is the site of mitotic phosphorylation of human thymidine kinase. J. Biol. Chem. 273: 12095-12100.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12095-12100
    • Chang, Z.F.1    Huang, D.Y.2    Chi, L.M.3
  • 11
    • 0023395549 scopus 로고
    • Control of thymidine kinase mRNA during the cell cycle
    • Coppock, D.L. and Pardee, A.B. 1987. Control of thymidine kinase mRNA during the cell cycle. Mol. Cell. Biol. 7: 2925-2932.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2925-2932
    • Coppock, D.L.1    Pardee, A.B.2
  • 12
    • 0029144015 scopus 로고
    • Molecular analysis of mutations in hprt gene of V79 hamster fibroblasts: Effects of imbalances in the dCTP, dGTP, and dTTP pools
    • Dare, E., Zhang, L.H., Jenssen, D., and Bianchi, V. 1995. Molecular analysis of mutations in hprt gene of V79 hamster fibroblasts: Effects of imbalances in the dCTP, dGTP, and dTTP pools. J. Mol. Biol. 252: 514-521.
    • (1995) J. Mol. Biol. , vol.252 , pp. 514-521
    • Dare, E.1    Zhang, L.H.2    Jenssen, D.3    Bianchi, V.4
  • 13
    • 0029049577 scopus 로고
    • Cellular targets for activation by the E2F1 transcription factor include DNA synthesis- and G1/S-regulatory genes
    • DeGregori, J., Kowalik T., and Nevins, J.R. 1995. Cellular targets for activation by the E2F1 transcription factor include DNA synthesis- and G1/S-regulatory genes. Mol. Cell. Biol. 8: 4215-4224.
    • (1995) Mol. Cell. Biol. , vol.8 , pp. 4215-4224
    • DeGregori, J.1    Kowalik, T.2    Nevins, J.R.3
  • 15
    • 0018786927 scopus 로고
    • Allosteric regulation of calf thymus ribonucleoside diphosphate reductase
    • Eriksson, S., Thelander, L., and Akerman, M. 1979. Allosteric regulation of calf thymus ribonucleoside diphosphate reductase. Biochemistry 18: 2948-2952.
    • (1979) Biochemistry , vol.18 , pp. 2948-2952
    • Eriksson, S.1    Thelander, L.2    Akerman, M.3
  • 16
    • 0036713310 scopus 로고    scopus 로고
    • The anaphase-promoting complex: It's not just for mitosis any more
    • Harper, J.W., Burton, J.L., and Solomon, M.J. 2002. The anaphase-promoting complex: It's not just for mitosis any more. Genes & Dev. 16: 2179-2206.
    • (2002) Genes & Dev. , vol.16 , pp. 2179-2206
    • Harper, J.W.1    Burton, J.L.2    Solomon, M.J.3
  • 17
    • 0027931438 scopus 로고
    • Human dTMP kinase: Gene expression and enzymatic activity coinciding with cell cycle progression and cell growth
    • Huang, S.H., Tang, A., Drisco, B., Zhang, S.Q., Seeger, R., Li, C., and Jong, A. 1994. Human dTMP kinase: Gene expression and enzymatic activity coinciding with cell cycle progression and cell growth. DNA Cell Biol. 13: 461-471.
    • (1994) DNA Cell Biol. , vol.13 , pp. 461-471
    • Huang, S.H.1    Tang, A.2    Drisco, B.3    Zhang, S.Q.4    Seeger, R.5    Li, C.6    Jong, A.7
  • 18
    • 0347986676 scopus 로고    scopus 로고
    • Mitotic degradation of human thymidine kinase 1 is dependent on the anaphase-promoting complex/cyclosome-Cdh1-mediated pathway
    • Ke, P.Y. and Chang, Z.F. 2004. Mitotic degradation of human thymidine kinase 1 is dependent on the anaphase-promoting complex/cyclosome-Cdh1-mediated pathway. Mol. Cell. Biol. 24: 514-526.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 514-526
    • Ke, P.Y.1    Chang, Z.F.2
  • 19
    • 0032488057 scopus 로고    scopus 로고
    • Activation of the human anaphase-promoting complex by proteins of the CDC20/Fizzy family
    • Kramer, E.R., Geiffers, C., Holzl, G., Hengstschlager, M., and Peters, J.M. 1998. Activation of the human anaphase-promoting complex by proteins of the CDC20/Fizzy family. Curr. Biol. 8: 1207-1210.
    • (1998) Curr. Biol. , vol.8 , pp. 1207-1210
    • Kramer, E.R.1    Geiffers, C.2    Holzl, G.3    Hengstschlager, M.4    Peters, J.M.5
  • 20
    • 0023746738 scopus 로고
    • Mutagenesis and deoxyribonucleotide pool imbalance
    • Kunz, B.A. 1988. Mutagenesis and deoxyribonucleotide pool imbalance. Mutat. Res. 200: 133-147.
    • (1988) Mutat. Res. , vol.200 , pp. 133-147
    • Kunz, B.A.1
  • 21
    • 0347694727 scopus 로고    scopus 로고
    • Perturbation of ATP-induced tetramerization of human cytosolic thymidine kinase by substitution of serine-13 with aspartic acid at the mitotic phosphorylation site
    • Li, J.L., Lu, C.Y., Ke, P.Y., and Chang, Z.F. 2004. Perturbation of ATP-induced tetramerization of human cytosolic thymidine kinase by substitution of serine-13 with aspartic acid at the mitotic phosphorylation site. Biochem. Biophys. Res. Commun. 313: 587-593.
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 587-593
    • Li, J.L.1    Lu, C.Y.2    Ke, P.Y.3    Chang, Z.F.4
  • 22
    • 0028800005 scopus 로고
    • Molecular characterization of the murine thymidylate kinase gene
    • Liang, P., Averboukh, L., Zhu, W., Haley, T., and Pardee, A.B. 1995. Molecular characterization of the murine thymidylate kinase gene. Cell Growth Differ. 6: 1333-1338.
    • (1995) Cell Growth Differ. , vol.6 , pp. 1333-1338
    • Liang, P.1    Averboukh, L.2    Zhu, W.3    Haley, T.4    Pardee, A.B.5
  • 23
    • 0036714512 scopus 로고    scopus 로고
    • Identification of a new APC/C recognition domain, the A box, which is required for the Cdh1-dependent destruction of the kinase Aurora-A during mitotic exit
    • Littlepage, L.E. and Ruderman, J.V. 2002. Identification of a new APC/C recognition domain, the A box, which is required for the Cdh1-dependent destruction of the kinase Aurora-A during mitotic exit. Genes & Dev. 16: 2274-2285.
    • (2002) Genes & Dev. , vol.16 , pp. 2274-2285
    • Littlepage, L.E.1    Ruderman, J.V.2
  • 24
    • 0036316015 scopus 로고    scopus 로고
    • Different roles for nonhomologous end joining and homologous recombination following replication arrest in mammalian cells
    • Lundin, C., Erixon, K., Arnaudeau, C., Schultz, N., Jenssen, D., Meuth, M., and Helleday, T. 2002. Different roles for nonhomologous end joining and homologous recombination following replication arrest in mammalian cells. Mol. Cell. Biol. 22: 5869-5878.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5869-5878
    • Lundin, C.1    Erixon, K.2    Arnaudeau, C.3    Schultz, N.4    Jenssen, D.5    Meuth, M.6    Helleday, T.7
  • 25
    • 0024505072 scopus 로고
    • The molecular basis of mutations induced by deoxyribonucleoside triphosphate pool imbalances in mammalian cells
    • Meuth, M. 1989. The molecular basis of mutations induced by deoxyribonucleoside triphosphate pool imbalances in mammalian cells. Exp. Cell Res. 181: 305-316.
    • (1989) Exp. Cell Res. , vol.181 , pp. 305-316
    • Meuth, M.1
  • 26
    • 0036711812 scopus 로고    scopus 로고
    • Defects in homologous recombination repair in mismatch-repair-deficient tumour cell lines
    • Mohindra, A., Hays, L.E., Phillips, E.N., Preston, B.D., Helleday, T., and Meuth, M. 2002. Defects in homologous recombination repair in mismatch-repair-deficient tumour cell lines. Hum. Mol. Genet. 11: 2189-2200.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2189-2200
    • Mohindra, A.1    Hays, L.E.2    Phillips, E.N.3    Preston, B.D.4    Helleday, T.5    Meuth, M.6
  • 27
    • 1642474203 scopus 로고    scopus 로고
    • A tumour-derived mutant allele of XRCC2 preferentially suppresses homologous recombination at DNA replication forks
    • Mohindra, A., Bolderson, E., Stone, J., Wells, M., Helleday, T., and Meuth, M. 2004. A tumour-derived mutant allele of XRCC2 preferentially suppresses homologous recombination at DNA replication forks. Hum. Mol. Genet. 13: 203-212.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 203-212
    • Mohindra, A.1    Bolderson, E.2    Stone, J.3    Wells, M.4    Helleday, T.5    Meuth, M.6
  • 28
    • 0019321438 scopus 로고
    • Cell cycle regulation of thymidylate synthetase gene expression in cultured mouse fibroblasts
    • Navalgund, L.G., Rossana, C., Muench, A.J., and Johnson, L.F. 1980. Cell cycle regulation of thymidylate synthetase gene expression in cultured mouse fibroblasts. J. Biol. Chem. 255: 7386-7390.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7386-7390
    • Navalgund, L.G.1    Rossana, C.2    Muench, A.J.3    Johnson, L.F.4
  • 29
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: Proteolysis in mitosis and beyond
    • Peters, J.M. 2002. The anaphase-promoting complex: Proteolysis in mitosis and beyond. Mol. Cell 9: 931-943.
    • (2002) Mol. Cell , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 31
    • 0034654399 scopus 로고    scopus 로고
    • The KEN box: An APC recognition signal distinct from the D box targeted by Cdh1
    • Pfleger, C.M. and Kirschner, M.W. 2000. The KEN box: An APC recognition signal distinct from the D box targeted by Cdh1. Genes & Dev. 14: 655-665.
    • (2000) Genes & Dev. , vol.14 , pp. 655-665
    • Pfleger, C.M.1    Kirschner, M.W.2
  • 32
    • 0035883946 scopus 로고    scopus 로고
    • Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex
    • Pfleger, C.M., Lee, E., and Kirschner, M.W. 2001. Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex. Genes & Dev. 15: 2396-2407.
    • (2001) Genes & Dev. , vol.15 , pp. 2396-2407
    • Pfleger, C.M.1    Lee, E.2    Kirschner, M.W.3
  • 33
    • 0023925454 scopus 로고
    • Interactions between deoxyribonulceotide and DNA synthesis
    • Reichard, P. 1988. Interactions between deoxyribonulceotide and DNA synthesis. Annu. Rev. Biochem. 57: 349-374.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 349-374
    • Reichard, P.1
  • 34
    • 0034693148 scopus 로고    scopus 로고
    • Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase
    • Reichard, P., Eliasson, R., Ingemarson, R., and Thelander, L. 2000. Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase. J. Biol. Chem. 275: 33021-33026.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33021-33026
    • Reichard, P.1    Eliasson, R.2    Ingemarson, R.3    Thelander, L.4
  • 35
    • 0038329967 scopus 로고
    • Yeast gene CDC8 encodes thymidylate kinase and is complemented by herpes thymidine kinase gene TK
    • Sclafani, R.A. and Fangman, W.L. 1984. Yeast gene CDC8 encodes thymidylate kinase and is complemented by herpes thymidine kinase gene TK. Proc. Natl. Acad. Sci. 81: 5821-5825.
    • (1984) Proc. Natl. Acad. Sci. , vol.81 , pp. 5821-5825
    • Sclafani, R.A.1    Fangman, W.L.2
  • 36
    • 0023951483 scopus 로고
    • Regulation of human thymidine kinase during the cell cycle
    • Sherley, J.L. and Kelly, T.J. 1988. Regulation of human thymidine kinase during the cell cycle. J. Biol. Chem. 263: 8350-8358.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8350-8358
    • Sherley, J.L.1    Kelly, T.J.2
  • 37
    • 0024402491 scopus 로고
    • Enzymatic assay for deoxyribonucleoside triphosphates using synthetic oligonucleotides as template primers
    • Sherman, P.A. and Fyfe, J.A. 1989. Enzymatic assay for deoxyribonucleoside triphosphates using synthetic oligonucleotides as template primers. Anal. Biochem. 180: 222-226.
    • (1989) Anal. Biochem. , vol.180 , pp. 222-226
    • Sherman, P.A.1    Fyfe, J.A.2
  • 38
    • 0023710414 scopus 로고
    • Dynamic of the thymidine triphosphate pool during the cell cycle of synchronized 3T3 mouse fibroblast
    • Spyrou, G. and Reichard, P. 1988. Dynamic of the thymidine triphosphate pool during the cell cycle of synchronized 3T3 mouse fibroblast. Mutat. Res. 200: 37-43.
    • (1988) Mutat. Res. , vol.200 , pp. 37-43
    • Spyrou, G.1    Reichard, P.2
  • 39
    • 0014503351 scopus 로고
    • Thymidine as a synchronizing agent I. Nucleic acid and protein formation in synchronous HeLa cultures treated with excess thymidine
    • Studzinski, G.P. and Lambert, W.C. 1969. Thymidine as a synchronizing agent I. Nucleic acid and protein formation in synchronous HeLa cultures treated with excess thymidine. J. Cell Physiol. 73: 109-117.
    • (1969) J. Cell Physiol. , vol.73 , pp. 109-117
    • Studzinski, G.P.1    Lambert, W.C.2
  • 40
    • 0025969987 scopus 로고
    • Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast
    • Su, J.Y. and Sclafani, R.A. 1991. Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast. Nucleic Acids Res. 10: 459-472.
    • (1991) Nucleic Acids Res. , vol.10 , pp. 459-472
    • Su, J.Y.1    Sclafani, R.A.2
  • 41
    • 1642399624 scopus 로고    scopus 로고
    • Degradation of the SCF component Skp2 in cell cycle phase G1 by anaphase-promoting complex
    • Wei, W., Ayad, N.G., Wan, Y., Zhang, G.J., Kirschner, M.W., and Kaellin Jr., W.G. 2004. Degradation of the SCF component Skp2 in cell cycle phase G1 by anaphase-promoting complex. Nature 428: 194-198.
    • (2004) Nature , vol.428 , pp. 194-198
    • Wei, W.1    Ayad, N.G.2    Wan, Y.3    Zhang, G.J.4    Kirschner, M.W.5    Kaellin Jr., W.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.