AP-site cleavage activity of tyrosyl-DNA phosphodiesterase 1

Лебедева, Н. А.; Rechkunova, N. I.; Lavrik, Olga I.

doi:10.1016/j.febslet.2011.01.032

Cited by 92 publications

(66 citation statements)

References 15 publications

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“…The importance of TDP1 outside Top1cc repair was first shown for 3′-phosphoglycolate ends and 3′-deoxyribose phosphate ends (Fig. 3E), which are common products of oxidative DNA damage as well as from radiomimetic drugs such as bleomycin [45,52,61–65]. Accordingly, TDP1 knockout cells are deficient in repairing oxidative DNA damage both in mitochondria and the nucleus [43,66,67].…”

Section: Tyrosyl-dna Phosphodiesterase 1 (Tdp1)mentioning

confidence: 99%

“…TDP1 also efficiently hydrolyzes 3′-deoxyribose lesions resulting from base alkylation after AP lyase processing [45,65]. This activity is particularly relevant for the repair of DNA lesions induced by monofunctional alkylating agents including methylmethanesulfonate and temozolomide, and ionizing radiations [45,53].…”

Section: Tyrosyl-dna Phosphodiesterase 1 (Tdp1)mentioning

confidence: 99%

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Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2)

et al. 2014

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TDP1 and TDP2 were discovered and named based on the fact they process 3′- and 5′-DNA ends by excising irreversible protein tyrosyl-DNA complexes involving topoisomerases I and II, respectively. Yet, both enzymes have an extended spectrum of activities. TDP1 not only excises trapped topoisomerases I (Top1 in the nucleus and Top1mt in mitochondria), but also repairs oxidative damage-induced 3′-phosphoglycolates and alkylation damage-induced DNA breaks, and excises chain terminating anticancer and antiviral nucleosides in the nucleus and mitochondria. The repair function of TDP2 is devoted to the excision of topoisomerase II- and potentially topoisomerases III-DNA adducts. TDP2 is also essential for the life cycle of picornaviruses (important human and bovine pathogens) as it unlinks VPg proteins from the 5′-end of the viral RNA genome. Moreover, TDP2 has been involved in signal transduction (under the former names of TTRAP or EAPII). The DNA repair partners of TDP1 include PARP1, XRCC1, ligase III and PNKP from the base excision repair (BER) pathway. By contrast, TDP2 repair functions are coordinated with Ku and ligase IV in the non-homologous end joining pathway (NHEJ). This article summarizes and compares the biochemistry, functions, and post-translational regulation of TDP1 and TDP2, as well as the relevance of TDP1 and TDP2 as determinants of response to anticancer agents. We discuss the rationale for developing TDP inhibitors for combinations with topoisomerase inhibitors (topotecan, irinotecan, doxorubicin, etoposide, mitoxantrone) and DNA damaging agents (temozolomide, bleomycin, cytarabine, and ionizing radiation), and as novel antiviral agents.

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Section: Tyrosyl-dna Phosphodiesterase 1 (Tdp1)mentioning

confidence: 99%

Section: Tyrosyl-dna Phosphodiesterase 1 (Tdp1)mentioning

confidence: 99%

Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2)

et al. 2014

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“…CPTs, which include the Food and Drug Administration-approved analogs topotecan and irinotecan, reversibly stabilize the covalent Top1-DNA complex to induce S phase-specific lethal DNA lesions (2)(3)(4)(5)(6). More recently, Tdp1 has been shown to process a wide range of other DNA adducts, including 3Ј-modified nucleotides, such as phosphoglycolates and chain-terminating nucleotides, and a 3Ј-phosphohistidyl intermediate formed during Tdp1 catalysis (7)(8)(9)(10)(11)(12)(13).…”

Section: Tyrosyl-dna Phosphodiesterase I (Tdp1)mentioning

confidence: 99%

Tyrosyl-DNA Phosphodiesterase I Catalytic Mutants Reveal an Alternative Nucleophile That Can Catalyze Substrate Cleavage

Comeaux

Cuya

Kojima

et al. 2015

Journal of Biological Chemistry

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“…Tdp1 can also process protruding 3'-phosphoglycolate termini on DSBs (Inamdar et al, 2002) and cleave phosphoamide bonds (Interthal et al, 2001). The enzyme participates in non-homologous end joining (NHEJ) (Bahmed et al, 2010) and base excision repair (BER) (Lebedeva et al, 2011). The expanding literature on the Tdp1 function has revealed that animal systems possess either DNA repair pathways able to remove the stabilized topo I-DNA covalent complexes in parallel with the Tdp1-mediated repair pathway or alternative DNA repair pathways which are activated in the Tdp1-depleted cells.…”

Section: Introductionmentioning

confidence: 99%

RNA-Seq analysis discloses early senescence and nucleolar dysfunction triggered by Tdp1α depletion in Medicago truncatula

Donà¹,

Confalonieri

Minio

et al. 2013

Journal of Experimental Botany

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An intron-spliced hairpin RNA approach was used for the targeted silencing of the MtTdp1α gene encoding the αisoform of tyrosyl-DNA phosphodiesterase 1 in Medicago truncatula Gaertn. Tyrosyl-DNA phosphodiesterase 1, involved in the repair of DNA topoisomerase I-mediated DNA damage, has been poorly investigated in plants. RNASeq analysis, carried out in the MtTdp1α-depleted plants, revealed different levels of transcriptional modulation (up-and down-regulation, alternative splicing, activation of alternative promoter) in genes involved in DNA damage sensing, DNA repair, and chromatin remodelling. It is suggested that the MtTdp1α gene has new, previously undetected roles in maintaining genome integrity. Up-regulation of senescence-associated genes and telomere shortening were observed. Moreover, impaired ribosome biogenesis indicated that the MtTdp1α gene is required for the nucleolar function. In agreement with the RNA-Seq data, transmission electron microscopy detected an altered nucleolar architecture in the MtTdp1α-depleted cells. Based on the reported data, a working hypothesis related to the occurrence of a nucleolar checkpoint in plant cells is proposed.

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AP-site cleavage activity of tyrosyl-DNA phosphodiesterase 1

Cited by 92 publications

References 15 publications

Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2)

Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2)

Tyrosyl-DNA Phosphodiesterase I Catalytic Mutants Reveal an Alternative Nucleophile That Can Catalyze Substrate Cleavage

RNA-Seq analysis discloses early senescence and nucleolar dysfunction triggered by Tdp1α depletion in Medicago truncatula

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