Structural insights on the small subunit of DNA topoisomerase I from the unicellular parasite Leishmania donovani

Biochimie

Volumn 89, Issue 12, 2007, Pages 1517-1527

  Díaz González, Rosario ^a   Pérez Pertejo, Yolanda ^a   Redondo, Carmen M ^a   Pommier, Yves ^b   Balaña Fouce, Rafael ^a   Reguera, Rosa M ^a  

^a UNIVERSITY OF LEÓN   (Spain)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Camptothecin; DNA topoisomerase IB; Leishmania donovani; Tropical diseases; Trypanosomatids

Indexed keywords

CAMPTOTHECIN; DNA TOPOISOMERASE; DNA TOPOISOMERASE IB; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DNA CLEAVAGE; DNA DENATURATION; DNA REPAIR; DNA REPLICATION; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBUNIT; LEISHMANIA DONOVANI; NONHUMAN; NUCLEOTIDE SEQUENCE; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; CAMPTOTHECIN; CLONING, MOLECULAR; DNA; DNA TOPOISOMERASES, TYPE I, EUKARYOTIC; DOSE-RESPONSE RELATIONSHIP, DRUG; GENE DELETION; LEISHMANIA DONOVANI; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PROTOZOAN PROTEINS; SACCHAROMYCES CEREVISIAE;

LEISHMANIA DONOVANI; TRYPANOSOMATIDAE;

EID: 36248959720     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2007.07.015     Document Type: Article

References (33)

1. Herwaldt B.L. Leishmaniasis. Lancet 354 (1999) 1191-1199
2. Murray H.W., Berman J.D., Davies C.R., and Saravia N.G. Advances in leishmaniasis. Lancet 366 (2005) 1561-1577
3. Burton A. Sharing needles may produce artificial leishmaniasis cycle. Lancet Infect. Dis. 1 (2001) 4
4. Champoux J.J. DNA topoisomerases: structure, function, and mechanism. Annu. Rev. Biochem. 70 (2001) 369-413
5. Wang J.C. Cellular roles of DNA topoisomerases: a molecular perspective. Nat. Rev. Mol. Cell Biol. 3 (2002) 430-444
6. Corbett K.D., and Berger J.M. Structure, molecular mechanisms, and evolutionary relationships in DNA topoisomerases. Annu. Rev. Biophys. Biomol. Struct. 33 (2004) 95-118
7. Pommier Y., Redon C., Rao V.A., Seiler J.A., Sordet O., Takemura H., Antony S., Meng L., Liao Z., Kohlhagen G., Zhang H., and Kohn K.W. Repair of and checkpoint response to topoisomerase I-mediated DNA damage. Mutat. Res. 532 (2003) 173-203
8. Leppard J.B., and Champoux J.J. Human DNA topoisomerase I: relaxation, roles, and damage control. Chromosoma 114 (2005) 75-85
9. Stewart L., Redinbo M.R., Qiu X., Hol W.G., and Champoux J.J. A model for the mechanism of human topoisomerase I. Science 279 (1998) 1534-1541
10. Stewart L., Ireton G.C., and Champoux J.J. The domain organization of human topoisomerase I. J. Biol. Chem. 271 (1996) 7602-7608
11. Redinbo M.R., 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
12. 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
13. Villa H., Otero Marcos A.R., Reguera R.M., Balaña-Fouce R., García-Estrada C., Pérez-Pertejo Y., Tekwani B.L., Myler P.J., Stuart K.D., Bjornsti M.A., and Ordóñez D. A novel active DNA topoisomerase I in Leishmania donovani. J. Biol. Chem. 278 (2003) 3521-3526
14. Bodley A.L., Chakraborty A.K., Xie S., Burri C., and Shapiro T.A. An unusual type IB topoisomerase from African trypanosomes. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 7539-7544
15. Balaña-Fouce R., Redondo C.M., Pérez-Pertejo Y., Díaz-González R., and Reguera R.M. Targeting atypical trypanosomatid DNA topoisomerase I. Drug Discov. Today 11 (2006) 733-740
16. Reguera R.M., Redondo C.M., Gutiérrez de Prado R., Pérez-Pertejo Y., and Balaña-Fouce R. DNA topoisomerase I from parasitic protozoa: a potential target for chemotherapy. Biochim. Biophys. Acta 1759 (2006) 117-131
17. 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
18. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning A Laboratory Manual (1989), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
19. Altschul S.F., Madden T.L., Schäffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 (1997) 3389-3402
20. Gietz R.D., and Schiestl R.H. Applications of high efficiency lithium acetate transformation of intact yeast cells using single-stranded nucleic acids as carrier. Yeast 7 (1991) 253-263
21. Jazwinski S.M. Preparation of extracts from yeast. Methods Enzymol. 182 (1990) 154-174
22. Bradford M.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
23. 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
24. Antony S., Jayaraman M., Laco G., Kohlhagen G., Kohn K.W., Cushman M., and Pommier Y. Differential induction of topoisomerase I-DNA cleavage complexes by the indenoisoquinoline MJ-III-65 (NSC 706744) and camptothecin: base sequence analysis and activity against camptothecin-resistant topoisomerases I. Cancer Res. 63 (2003) 7428-7435
25. Stewart L., Ireton G.C., and Champoux J.J. Reconstitution of human topoisomerase I by fragment complementation. J. Mol. Biol. 269 (1997) 355-372
26. Park H., and Sternglanz R. Two separate conserved domains of eukaryotic DNA topoisomerase I bind to each other and reconstitute enzymatic activity. Chromosoma 107 (1998) 211-215
27. Davies D.R., 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
28. Porter S.E., and Champoux J.J. The basis for camptothecin enhancement of DNA breakage by eukaryotic topoisomerase I. Nucleic Acids Res. 11 (1989) 8521-8532
29. Ireton G.C., Stewart L., Parker L.H., and Champoux J.J. Expression of human topoisomerase I with a partial deletion of the linker region yields monomeric and dimeric enzymes that respond differently to camptothecin. J. Biol. Chem. 275 (2000) 25820-25830
30. Das B.B., Dasgupta S.D., Ganguly A., Mazumder S., Roy A., and Majumder H.K. Leishmania donovani bisubunit topoisomerase I gene fusion leads to an active enzyme with conserved type IB enzyme function. FEBS J. 274 (2007) 150-163
31. Desai S.D., Liu L.F., Vazquez-Abad D., and D'Arpa P. Ubiquitin-dependent destruction of topoisomerase I is stimulated by the antitumor drug camptothecin. J. Biol. Chem. 272 (1997) 24159-24164
32. Desai S.D., Li T.K., Rodríguez-Bauman A., Rubin E.H., and Liu L.F. Ubiquitin/26S proteasome-mediated degradation of topoisomerase I as a resistance mechanism to camptothecin in tumor cells. Cancer Res. 61 (2001) 5926-5932
33. Pommier Y. Camptothecins and topoisomerase I: a foot in the door. Targeting the genome beyond topoisomerase I with camptothecins and novel anticancer drugs: importance of DNA replication, repair and cell cycle checkpoints. Curr. Med. Chem. Anticancer Agents 4 (2004) 429-434