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Tyrosyl-DNA phosphodiesterase 1

Tdp1, tyrosyl-DNA phosphodiesterase, Tyrosyl-DNA phosphodiesterase 1, tyrosyl-DNA phosphodiesterase I
The protein encoded by this gene is involved in repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. This protein may also remove glycolate from single-stranded DNA containing 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks. This gene is a member of the phospholipase D family and contains two PLD phosphodiesterase domains. Mutations in this gene are associated with the disease spinocerebellar ataxia with axonal neuropathy (SCAN1). While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode the same isoform. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Phosphodiesterase, DNA topoisomerase I, CAN, POLYMERASE, XRCC1
Papers on Tdp1
FEN1 participates in repair of the 5'-phosphotyrosyl terminus of DNA single-strand breaks.
Kuraoka et al., Suita, Japan. In Carcinogenesis, Jan 2016
Human tyrosyl-DNA phosphodiesterase 2 (TDP2) is required for efficient repair of Top2-DSB complexes.
Depletion of tyrosyl-DNA phosphodiesterase 1α (MtTdp1α) affects transposon expression in Medicago truncatula.
Balestrazzi et al., Pavia, Italy. In J Integr Plant Biol, Jan 2016
UNASSIGNED: The role of plant tyrosyl-DNA phosphodiesterase 1α in genome stability is studied using a Medicago truncatula MtTdp1α-depleted line.
A transcription-independent epigenetic mechanism is associated with antigenic switching in Trypanosoma brucei.
Figueiredo et al., Lisbon, Portugal. In Nucleic Acids Res, Jan 2016
This conformation is independent of the cell-cycle stage, but dependent upon TDP1, a high mobility group box protein.
DNA-PK triggers histone ubiquitination and signaling in response to DNA double-strand breaks produced during the repair of transcription-blocking topoisomerase I lesions.
Sordet et al., Toulouse, France. In Nucleic Acids Res, Dec 2015
Stabilized topoisomerase I cleavage complexes (Top1cc) by natural compounds or common DNA alterations are transcription-blocking lesions whose repair depends primarily on Top1 proteolysis and excision by tyrosyl-DNA phosphodiesterase-1 (TDP1).
Tyrosyl-DNA-phosphodiesterase I (TDP1) participates in the removal and repair of stabilized-Top2α cleavage complexes in human cells.
de Campos Nebel et al., Buenos Aires, Argentina. In Mutat Res, Nov 2015
Tyrosyl-DNA-phosphodiesterase 1 (TDP1) is a DNA repair enzyme that removes irreversible protein-linked 3' DNA complexes, 3' phosphoglycolates, alkylation damage-induced DNA breaks, and 3' deoxyribose nucleosides.
[Tyrosyl-DNA Phosphodiesterase 1 Is a New Player in Repair of Apurinic/Apyrimidinic Sites].
Lavrik et al., In Bioorg Khim, Sep 2015
This review is dedicated to one of these proteins, tyrosyl-DNA phosphodiesterase 1 (Tdp1), for which we have recently shown that in addition to its main activity of specific cleavage of the tyrosyl-DNA bond formed via a covalent attachment of topoisomerase 1 (Top1) to DNA, Tdp1 is able to initiate the cleavage of the internal AP sites in DNA and their following repair.
Abacavir, an anti-HIV-1 drug, targets TDP1-deficient adult T cell leukemia.
Takaori-Kondo et al., Kyoto, Japan. In Sci Adv, Apr 2015
We found that the reduced expression of tyrosyl-DNA phosphodiesterase 1 (TDP1), a repair enzyme, is attributable to the cytotoxic effect of abacavir on ATL cells.
Recognition and repair of chemically heterogeneous structures at DNA ends.
Williams et al., United States. In Environ Mol Mutagen, 2015
These nucleic acid transactions employ direct damage reversal enzymes including Aprataxin (APTX), Polynucleotide kinase phosphatase (PNK), the tyrosyl DNA phosphodiesterases (TDP1 and TDP2), the Ku70/80 complex and DNA polymerase β (POLβ).
Divergent Requirement for a DNA Repair Enzyme during Enterovirus Infections.
Semler et al., Irvine, United States. In Mbio, 2014
One of these host proteins is a cellular DNA repair enzyme known as 5' tyrosyl-DNA phosphodiesterase 2 (TDP2).
Tyrosyl-DNA phosphodiesterase I resolves both naturally and chemically induced DNA adducts and its potential as a therapeutic target.
van Waardenburg et al., Birmingham, United States. In Drug Metab Rev, 2014
Tyrosyl-DNA phosphodiesterase I (Tdp1) is a eukaryotic DNA repair enzyme that catalyzes the removal of covalent 3'-DNA adducts.
Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2).
Marchand et al., Bethesda, United States. In Dna Repair (amst), 2014
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.
The role of TDP1 and APTX in mitochondrial DNA repair.
Lightowlers et al., Newcastle upon Tyne, United Kingdom. In Biochimie, 2014
In this short review two enzymes, tyrosyl-DNA-phosphodiesterase 1 (TDP1) and aprataxin (APTX), involved in mitochondrial single strand break repair (SSBR) are discussed.
Tyrosyl-DNA phosphodiesterase 1 (TDP1) repairs DNA damage induced by topoisomerases I and II and base alkylation in vertebrate cells.
Pommier et al., Kyoto, Japan. In J Biol Chem, 2012
Our findings reveal a broad involvement of Tdp1 in DNA repair and clarify the role of human TDP1 in the repair of Top2-induced DNA damage.
Analysis of the active-site mechanism of tyrosyl-DNA phosphodiesterase I: a member of the phospholipase D superfamily.
van Waardenburg et al., Memphis, United States. In J Mol Biol, 2012
Analysis of the active-site mechanism of tyrosyl-DNA phosphodiesterase I.
SUMO modification of the neuroprotective protein TDP1 facilitates chromosomal single-strand break repair.
El-Khamisy et al., Brighton, United Kingdom. In Nat Commun, 2011
study identifies TDP1 as a target for modification by the small ubiquitin-like modifier SUMO and provides evidence implicating SUMOylation in facilitating TDP1 cellular function during single-strand break repair
Topoisomerase 1 and single-strand break repair modulate transcription-induced CAG repeat contraction in human cells.
Wilson et al., Houston, United States. In Mol Cell Biol, 2011
topoisomerase 1, tyrosyl-DNA phosphodiesterase 1, and single-strand break repair modulate transcription-dependent CAG repeat contractions
AP-site cleavage activity of tyrosyl-DNA phosphodiesterase 1.
Lavrik et al., Novosibirsk, Russia. In Febs Lett, 2011
Study investigates substrate specificity of Tdp1; data suggest a role for Tdp1 in a new APE-independent base excision repair pathway.
A human 5'-tyrosyl DNA phosphodiesterase that repairs topoisomerase-mediated DNA damage.
Caldecott et al., Brighton, United Kingdom. In Nature, 2009
The importance of liberating DNA termini from trapped topoisomerase is illustrated by the progressive neurodegenerative disease observed in individuals containing a mutation in tyrosyl-DNA phosphodiesterase 1 (TDP1), an enzyme that cleaves 3'-phosphotyrosyl bonds.
Defective DNA single-strand break repair in spinocerebellar ataxia with axonal neuropathy-1.
Caldecott et al., Brighton, United Kingdom. In Nature, 2005
Spinocerebellar ataxia with axonal neuropathy-1 (SCAN1) is a neurodegenerative disease that results from mutation of tyrosyl phosphodiesterase 1 (TDP1).
Mutation of TDP1, encoding a topoisomerase I-dependent DNA damage repair enzyme, in spinocerebellar ataxia with axonal neuropathy.
Lupski et al., Houston, United States. In Nat Genet, 2002
loss-of-function mutations in TDP1 may cause spinocerebellar ataxia with axonal neuropathy either by interfering with DNA transcription or by inducing apoptosis in postmitotic neurons
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