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Volumn 76, Issue 5, 2008, Pages 608-619

Mutational study of the "catalytic tetrad" of DNA topoisomerase IB from the hemoflagellate Leishmania donovani: Role of Asp-353 and Asn-221 in camptothecin resistance

Author keywords

Camptothecin; Leishmania; Site directed mutagenesis; Topoisomerase IB; Tropical diseases; Trypanosomatids

Indexed keywords

CAMPTOTHECIN; DNA TOPOISOMERASE;

EID: 49149110065     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2008.06.019     Document Type: Article
Times cited : (17)

References (39)
  • 1
    • 0142258171 scopus 로고    scopus 로고
    • Leishmaniasis-current chemotherapy and recent advances in the search for novel drugs
    • Croft S., and Coombs G.H. Leishmaniasis-current chemotherapy and recent advances in the search for novel drugs. Trends Parasitol 19 (2003) 502-508
    • (2003) Trends Parasitol , vol.19 , pp. 502-508
    • Croft, S.1    Coombs, G.H.2
  • 2
    • 27744451508 scopus 로고    scopus 로고
    • Clinical status of agents being developed for leishmaniasis
    • Berman J. Clinical status of agents being developed for leishmaniasis. Exp Opin Invest Drugs 14 (2005) 1337-1346
    • (2005) Exp Opin Invest Drugs , vol.14 , pp. 1337-1346
    • Berman, J.1
  • 4
    • 0034923502 scopus 로고    scopus 로고
    • DNA topoisomerases: structure, function, and mechanism
    • Champoux J.J. DNA topoisomerases: structure, function, and mechanism. Annu Rev Biochem 70 (2001) 369-413
    • (2001) Annu Rev Biochem , vol.70 , pp. 369-413
    • Champoux, J.J.1
  • 5
    • 2442599792 scopus 로고    scopus 로고
    • Structure, molecular mechanisms, and evolutionary relationships in DNA topoisomerases
    • Corbett K., and Berger J.M. Structure, molecular mechanisms, and evolutionary relationships in DNA topoisomerases. Annu Rev Biophys Biomol Struct 33 (2004) 95-118
    • (2004) Annu Rev Biophys Biomol Struct , vol.33 , pp. 95-118
    • Corbett, K.1    Berger, J.M.2
  • 6
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • Wang J. DNA topoisomerases. Annu Rev Biochem 65 (1996) 635-692
    • (1996) Annu Rev Biochem , vol.65 , pp. 635-692
    • Wang, J.1
  • 7
    • 0032489634 scopus 로고    scopus 로고
    • Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA
    • Redinbo M., Stewart L., Kuhn P., Champoux J.J., and Hol W.G. Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science 279 (1998) 1504-1513
    • (1998) Science , vol.279 , pp. 1504-1513
    • Redinbo, M.1    Stewart, L.2    Kuhn, P.3    Champoux, J.J.4    Hol, W.G.5
  • 8
    • 0029869828 scopus 로고    scopus 로고
    • The domain organization of DNA topoisomerase I
    • Stewart L., Ireton G.C., and Champoux J.J. The domain organization of DNA topoisomerase I. J Biol Chem 271 (1996) 7602-7608
    • (1996) J Biol Chem , vol.271 , pp. 7602-7608
    • Stewart, L.1    Ireton, G.C.2    Champoux, J.J.3
  • 9
    • 0032752373 scopus 로고    scopus 로고
    • A functional linker in human topoisomerase I is required for maximum sensitivity to camptothecin in a DNA relaxation assay
    • Stewart L., Ireton G.C., and Champoux J.J. A functional linker in human topoisomerase I is required for maximum sensitivity to camptothecin in a DNA relaxation assay. J Biol Chem 274 (1999) 32950-32960
    • (1999) J Biol Chem , vol.274 , pp. 32950-32960
    • Stewart, L.1    Ireton, G.C.2    Champoux, J.J.3
  • 13
    • 33750491962 scopus 로고    scopus 로고
    • Topoisomerases of kinetoplastid parasites: why so fascinating?
    • Das B.B., Sengupta T., Ganguly A., and Majumder H.K. Topoisomerases of kinetoplastid parasites: why so fascinating?. Mol Microbiol 62 (2006) 917-927
    • (2006) Mol Microbiol , vol.62 , pp. 917-927
    • Das, B.B.1    Sengupta, T.2    Ganguly, A.3    Majumder, H.K.4
  • 14
    • 0033634688 scopus 로고    scopus 로고
    • Catalytic mechanism of DNA topoisomerase IB
    • Krogh B., and Shuman S. Catalytic mechanism of DNA topoisomerase IB. Mol Cell Biol 5 (2000) 1035-1041
    • (2000) Mol Cell Biol , vol.5 , pp. 1035-1041
    • Krogh, B.1    Shuman, S.2
  • 15
    • 33644821060 scopus 로고    scopus 로고
    • The structure of the transition state of the heterodimeric topoisomerase I of Leishmania donovani as a vanadate complex with nicked DNA
    • Davies D., Mushtaq A., Interthal H., Champoux J.J., and Hol W.G. The structure of the transition state of the heterodimeric topoisomerase I of Leishmania donovani as a vanadate complex with nicked DNA. J Mol Biol 357 (2006) 1202-1210
    • (2006) J Mol Biol , vol.357 , pp. 1202-1210
    • Davies, D.1    Mushtaq, A.2    Interthal, H.3    Champoux, J.J.4    Hol, W.G.5
  • 16
    • 0026032557 scopus 로고
    • Molecular cloning of a cDNA of a camptothecin-resistant human DNA topoisomerase I and identification of mutation sites
    • Tamura H., Kohchi C., Yamada R., Ikeda T., Koiwai O., Patterson E., et al. Molecular cloning of a cDNA of a camptothecin-resistant human DNA topoisomerase I and identification of mutation sites. Nucl Acids Res 19 (1991) 69-75
    • (1991) Nucl Acids Res , vol.19 , pp. 69-75
    • Tamura, H.1    Kohchi, C.2    Yamada, R.3    Ikeda, T.4    Koiwai, O.5    Patterson, E.6
  • 17
    • 0027381388 scopus 로고
    • Mechanisms of camptothecin resistance in yeast DNA topoisomerase I mutants
    • Knab A., Fertala J., and Bjornsti M.A. Mechanisms of camptothecin resistance in yeast DNA topoisomerase I mutants. J Biol Chem 268 (1993) 22322-22330
    • (1993) J Biol Chem , vol.268 , pp. 22322-22330
    • Knab, A.1    Fertala, J.2    Bjornsti, M.A.3
  • 18
    • 16244400448 scopus 로고    scopus 로고
    • Topoisomerase I amino acid substitutions, Gly185Arg and Asp325Glu, confer camptothecin resistance in Leishmania donovani
    • Marquis J.F., Hardy I., and Olivier M. Topoisomerase I amino acid substitutions, Gly185Arg and Asp325Glu, confer camptothecin resistance in Leishmania donovani. Antimicrob Agents Chemother 49 (2005) 1441-1446
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1441-1446
    • Marquis, J.F.1    Hardy, I.2    Olivier, M.3
  • 19
    • 36248959720 scopus 로고    scopus 로고
    • Structural insights on the small subunit of DNA topoisomerase I from the unicellular parasite Leishmania donovani
    • Díaz-González R., Pérez-Pertejo Y., Redondo C.M., Pommier Y., Balaña-Fouce R., and Reguera R.M. Structural insights on the small subunit of DNA topoisomerase I from the unicellular parasite Leishmania donovani. Biochimie 89 (2007) 1517-1527
    • (2007) Biochimie , vol.89 , pp. 1517-1527
    • Díaz-González, R.1    Pérez-Pertejo, Y.2    Redondo, C.M.3    Pommier, Y.4    Balaña-Fouce, R.5    Reguera, R.M.6
  • 20
    • 0032553540 scopus 로고    scopus 로고
    • Intragenic suppressors of mutant DNA topoisomerase I-induced lethality diminish enzyme binding of DNA
    • Hann C.L., Carlberg A.L., and Bjornsti M.A. Intragenic suppressors of mutant DNA topoisomerase I-induced lethality diminish enzyme binding of DNA. J Biol Chem 273 (1998) 31519-31527
    • (1998) J Biol Chem , vol.273 , pp. 31519-31527
    • Hann, C.L.1    Carlberg, A.L.2    Bjornsti, M.A.3
  • 21
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul S.F., MaddenTL, Schäffer A.A., Zhang J., Zhang Z., Miller W., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucl Acids Res 25 (1997) 3389-3402
    • (1997) Nucl Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    MaddenTL2    Schäffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6
  • 23
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H., Fukuda Y., Murata K., and Kimura A. Transformation of intact yeast cells treated with alkali cations. J Bacteriol 153 (1983) 163-168
    • (1983) J Bacteriol , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 24
    • 0025255095 scopus 로고
    • Preparation of extracts from yeast
    • Jazwinski S.M. Preparation of extracts from yeast. Methods Enzymol 182 (1990) 154-174
    • (1990) Methods Enzymol , vol.182 , pp. 154-174
    • Jazwinski, S.M.1
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 26
    • 0021272096 scopus 로고
    • Identification of Saccharomyces cerevisiae mutants deficient in DNA topoisomerase I activity
    • Thrash C., Voelkel K., DiNardo S., and Sternglanz R. Identification of Saccharomyces cerevisiae mutants deficient in DNA topoisomerase I activity. J Biol Chem 259 (1984) 1375-1377
    • (1984) J Biol Chem , vol.259 , pp. 1375-1377
    • Thrash, C.1    Voelkel, K.2    DiNardo, S.3    Sternglanz, R.4
  • 27
    • 13444284042 scopus 로고    scopus 로고
    • Cellular topoisomerase I inhibition and antiproliferative activity by MJ-III-65 (NSC 706744), an indenoisoquinoline topoisomerase I poison
    • Antony S., Kohlhagen G., Agama K., Jayaraman M., Cao S., Durrani F.A., et al. Cellular topoisomerase I inhibition and antiproliferative activity by MJ-III-65 (NSC 706744), an indenoisoquinoline topoisomerase I poison. Mol Pharmacol 67 (2005) 523-530
    • (2005) Mol Pharmacol , vol.67 , pp. 523-530
    • Antony, S.1    Kohlhagen, G.2    Agama, K.3    Jayaraman, M.4    Cao, S.5    Durrani, F.A.6
  • 28
    • 0037040269 scopus 로고    scopus 로고
    • Active site mutations in DNA topoisomerase I distinguish the cytotoxic activities of camptothecin and the indolocarbazole, rebeccamycin
    • Woo M., Vance J.R., Marcos A.R., Bailly C., and Bjornsti M.A. Active site mutations in DNA topoisomerase I distinguish the cytotoxic activities of camptothecin and the indolocarbazole, rebeccamycin. J Biol Chem 277 (2002) 3813-3822
    • (2002) J Biol Chem , vol.277 , pp. 3813-3822
    • Woo, M.1    Vance, J.R.2    Marcos, A.R.3    Bailly, C.4    Bjornsti, M.A.5
  • 29
    • 0032518166 scopus 로고    scopus 로고
    • Replacement of the active site tyrosine of vaccinia DNA topoisomerase by glutamate, cysteine or histidine converts the enzyme into a site-specific endonuclease
    • Wittschieben J., Petersen B.O., and Shuman S. Replacement of the active site tyrosine of vaccinia DNA topoisomerase by glutamate, cysteine or histidine converts the enzyme into a site-specific endonuclease. Nucl Acids Res 26 (1998) 490-496
    • (1998) Nucl Acids Res , vol.26 , pp. 490-496
    • Wittschieben, J.1    Petersen, B.O.2    Shuman, S.3
  • 30
    • 1642453632 scopus 로고    scopus 로고
    • The role of lysine 532 in the catalytic mechanism of human topoisomerase I
    • Interthal H., Quigley P.M., Hol W.G., and Champoux J.J. The role of lysine 532 in the catalytic mechanism of human topoisomerase I. J Biol Chem 279 (2004) 2984-2992
    • (2004) J Biol Chem , vol.279 , pp. 2984-2992
    • Interthal, H.1    Quigley, P.M.2    Hol, W.G.3    Champoux, J.J.4
  • 31
    • 0029008048 scopus 로고
    • Molecular and cytotoxic effects of camptothecin, a topoisomerase I inhibitor, on trypanosomes and Leishmania
    • Bodley A.L., and Shapiro T.A. Molecular and cytotoxic effects of camptothecin, a topoisomerase I inhibitor, on trypanosomes and Leishmania. Proc Natl Acad Sci USA 92 (1995) 3726-3730
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3726-3730
    • Bodley, A.L.1    Shapiro, T.A.2
  • 33
    • 0024670218 scopus 로고
    • Peptide sequencing and site-directed mutagenesis identify tyrosine-727 as the active site tyrosine of Saccharomyces cerevisiae DNA topoisomerase I
    • Lynn R., Bjornsti M.A., Caron P.R., and Wang J.C. Peptide sequencing and site-directed mutagenesis identify tyrosine-727 as the active site tyrosine of Saccharomyces cerevisiae DNA topoisomerase I. Proc Natl Acad Sci USA 86 (1989) 3559-3563
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3559-3563
    • Lynn, R.1    Bjornsti, M.A.2    Caron, P.R.3    Wang, J.C.4
  • 34
    • 33750985385 scopus 로고    scopus 로고
    • The different cleavage DNA sequence specificity explains the camptothecin resistance of the human topoisomerase I Glu418Lys mutant
    • Fiorani P., Chillemi G., Losasso C., Castelli S., and Desideri A. The different cleavage DNA sequence specificity explains the camptothecin resistance of the human topoisomerase I Glu418Lys mutant. Nucl Acids Res 34 (2006) 5093-5100
    • (2006) Nucl Acids Res , vol.34 , pp. 5093-5100
    • Fiorani, P.1    Chillemi, G.2    Losasso, C.3    Castelli, S.4    Desideri, A.5
  • 35
    • 0242290326 scopus 로고    scopus 로고
    • Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I
    • Fiorani P., Bruselles A., Falconi M., Chillemi G., Desideri A., and Benedetti P. Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I. J Biol Chem 278 (2003) 43268-43275
    • (2003) J Biol Chem , vol.278 , pp. 43268-43275
    • Fiorani, P.1    Bruselles, A.2    Falconi, M.3    Chillemi, G.4    Desideri, A.5    Benedetti, P.6
  • 37
  • 38
    • 0030962069 scopus 로고    scopus 로고
    • Alterations in the catalytic activity of yeast DNA topoisomerase I result in cell cycle
    • Megonigal M., Fertala J., and Bjornsti M.A. Alterations in the catalytic activity of yeast DNA topoisomerase I result in cell cycle. J Biol Chem 272 (1997) 12801-12808
    • (1997) J Biol Chem , vol.272 , pp. 12801-12808
    • Megonigal, M.1    Fertala, J.2    Bjornsti, M.A.3
  • 39
    • 0035863393 scopus 로고    scopus 로고
    • Use of camptothecin-resistant mammalian cell lines to evaluate the role of topoisomerase I in the antiproliferative activity of the indolocarbazole, NB-506, and its topoisomerase I binding site
    • Urasaki Y., Laco G., Takebayashi Y., Bailly C., Kohlhagen G., and Pommier Y. Use of camptothecin-resistant mammalian cell lines to evaluate the role of topoisomerase I in the antiproliferative activity of the indolocarbazole, NB-506, and its topoisomerase I binding site. Cancer Res 61 (2001) 504-508
    • (2001) Cancer Res , vol.61 , pp. 504-508
    • Urasaki, Y.1    Laco, G.2    Takebayashi, Y.3    Bailly, C.4    Kohlhagen, G.5    Pommier, Y.6


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