Inhibition of Flp Recombinase by the Topoisomerase I-targeting Drugs, Camptothecin and NSC-314622

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Standard

Inhibition of Flp Recombinase by the Topoisomerase I-targeting Drugs, Camptothecin and NSC-314622. / From Frøhlich, Rikke; Hansen, Stefan Gude; Lisby, Michael; Grainge, Ian; Westergaard, Ole; Jayaram, Makkuni; Knudsen, Birgitta Ruth.

I: Journal of Biological Chemistry, Bind 276, Nr. 10, 09.03.2001, s. 6993-6997.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

From Frøhlich, R, Hansen, SG, Lisby, M, Grainge, I, Westergaard, O, Jayaram, M & Knudsen, BR 2001, 'Inhibition of Flp Recombinase by the Topoisomerase I-targeting Drugs, Camptothecin and NSC-314622', Journal of Biological Chemistry, bind 276, nr. 10, s. 6993-6997. https://doi.org/10.1074/jbc.C000901200

APA

From Frøhlich, R., Hansen, S. G., Lisby, M., Grainge, I., Westergaard, O., Jayaram, M., & Knudsen, B. R. (2001). Inhibition of Flp Recombinase by the Topoisomerase I-targeting Drugs, Camptothecin and NSC-314622. Journal of Biological Chemistry, 276(10), 6993-6997. https://doi.org/10.1074/jbc.C000901200

Vancouver

From Frøhlich R, Hansen SG, Lisby M, Grainge I, Westergaard O, Jayaram M o.a. Inhibition of Flp Recombinase by the Topoisomerase I-targeting Drugs, Camptothecin and NSC-314622. Journal of Biological Chemistry. 2001 mar. 9;276(10):6993-6997. https://doi.org/10.1074/jbc.C000901200

Author

From Frøhlich, Rikke ; Hansen, Stefan Gude ; Lisby, Michael ; Grainge, Ian ; Westergaard, Ole ; Jayaram, Makkuni ; Knudsen, Birgitta Ruth. / Inhibition of Flp Recombinase by the Topoisomerase I-targeting Drugs, Camptothecin and NSC-314622. I: Journal of Biological Chemistry. 2001 ; Bind 276, Nr. 10. s. 6993-6997.

Bibtex

@article{e79220a5ad8e4bf5bb68a6125f35532f,
title = "Inhibition of Flp Recombinase by the Topoisomerase I-targeting Drugs, Camptothecin and NSC-314622",
abstract = "Recombinases of the λ-Int family and type IB topoisomerases act by introducing transient single strand breaks in DNA using chemically identical reaction schemes. Recent structural data have supported the relationship between the two enzyme groups by revealing considerable similarities in the architecture of their catalytic pockets. In this study we show that the Int-type recombinase Flp is inhibited by the two structurally unrelated topoisomerase I-directed anti-cancer drugs, camptothecin (CPT) and NSC-314622. The interaction of these drugs with topoisomerase I is very specific with several single amino acid substitutions conferring drug resistance to the enzyme. Thus, the observed interaction of CPT and NSC-314622 with Flp, which is comparable to their interaction with the cleavage complex formed by topoisomerase I, strongly supports a close mechanistic and evolutionary relationship between the two enzymes. The results suggest that Flp and other Int family recombinases may provide model systems for dissecting the molecular mechanisms of topoisomerase I-directed anti-cancer therapeutic agents.",
author = "{From Fr{\o}hlich}, Rikke and Hansen, {Stefan Gude} and Michael Lisby and Ian Grainge and Ole Westergaard and Makkuni Jayaram and Knudsen, {Birgitta Ruth}",
year = "2001",
month = mar,
day = "9",
doi = "10.1074/jbc.C000901200",
language = "English",
volume = "276",
pages = "6993--6997",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "10",

}

RIS

TY - JOUR

T1 - Inhibition of Flp Recombinase by the Topoisomerase I-targeting Drugs, Camptothecin and NSC-314622

AU - From Frøhlich, Rikke

AU - Hansen, Stefan Gude

AU - Lisby, Michael

AU - Grainge, Ian

AU - Westergaard, Ole

AU - Jayaram, Makkuni

AU - Knudsen, Birgitta Ruth

PY - 2001/3/9

Y1 - 2001/3/9

N2 - Recombinases of the λ-Int family and type IB topoisomerases act by introducing transient single strand breaks in DNA using chemically identical reaction schemes. Recent structural data have supported the relationship between the two enzyme groups by revealing considerable similarities in the architecture of their catalytic pockets. In this study we show that the Int-type recombinase Flp is inhibited by the two structurally unrelated topoisomerase I-directed anti-cancer drugs, camptothecin (CPT) and NSC-314622. The interaction of these drugs with topoisomerase I is very specific with several single amino acid substitutions conferring drug resistance to the enzyme. Thus, the observed interaction of CPT and NSC-314622 with Flp, which is comparable to their interaction with the cleavage complex formed by topoisomerase I, strongly supports a close mechanistic and evolutionary relationship between the two enzymes. The results suggest that Flp and other Int family recombinases may provide model systems for dissecting the molecular mechanisms of topoisomerase I-directed anti-cancer therapeutic agents.

AB - Recombinases of the λ-Int family and type IB topoisomerases act by introducing transient single strand breaks in DNA using chemically identical reaction schemes. Recent structural data have supported the relationship between the two enzyme groups by revealing considerable similarities in the architecture of their catalytic pockets. In this study we show that the Int-type recombinase Flp is inhibited by the two structurally unrelated topoisomerase I-directed anti-cancer drugs, camptothecin (CPT) and NSC-314622. The interaction of these drugs with topoisomerase I is very specific with several single amino acid substitutions conferring drug resistance to the enzyme. Thus, the observed interaction of CPT and NSC-314622 with Flp, which is comparable to their interaction with the cleavage complex formed by topoisomerase I, strongly supports a close mechanistic and evolutionary relationship between the two enzymes. The results suggest that Flp and other Int family recombinases may provide model systems for dissecting the molecular mechanisms of topoisomerase I-directed anti-cancer therapeutic agents.

UR - http://www.scopus.com/inward/record.url?scp=0346409318&partnerID=8YFLogxK

U2 - 10.1074/jbc.C000901200

DO - 10.1074/jbc.C000901200

M3 - Journal article

C2 - 11152668

AN - SCOPUS:0346409318

VL - 276

SP - 6993

EP - 6997

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 10

ER -

ID: 241306141