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The role of conserved residues Y204, F259, S400 and W590 of the catalytic groove of TDP1 protein DNA cleavage activity was analyzed.
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We found the rs942190 GG genotype of TDP1 to be associated with relatively poor survival among small-cell lung cancer patients. Further investigation is needed to confirm the result and to determine whether this genotype may be a predictive marker for treatment efficacy of DNA topoisomerase inhibitors
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this study identifies the importance of TDP1 as a novel determinant of response to CNDAC across various cancer types (especially non-small cell lung cancers), and demonstrates the differential involvement of BRCA2, PARP1, and TDP1 in the cellular responses to CNDAC, AraC, and CPT
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Data indicate that the initial step of tyrosyl-DNA phosphodiesterase 1 (Tdp1) interaction with DNA includes binding of Tdp1 to the DNA ends followed by the 3'-nucleosidase reaction.
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Data indicate a molecular basis for DNA 3'-end processing by tyrosyl-DNA phosphodiesterase (Tdp1).
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Expression of human Tdp1HisnucAla and Tdp1HisgabAsn mutants results in stabilization of the covalent TDP1-DNA intermediate and induces cytotoxicity.
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We show that two genes, TDP1, a tyrosyl-DNA-phosphdiesterase, and TAF12, an RNA polymerase II TATA-box binding factor, cause CIN when overexpressed in human cells. Using SDL screens in yeast, we identified a set of genes that when deleted specifically kill cells with high levels of Tdp1
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TDP1 participation in human non-homologous end joining (NHEJ) is mediated by interaction with XLF, and that TDP1-XLF interactions and subsequent NHEJ events are regulated by phosphorylation of TDP1-S81.
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Mutations in TDP1 and APTX have been linked to Spinocerebellar ataxia with axonal neuropathy (SCAN1) and Ataxia-ocular motor apraxia 1 (AOA1), respectively, while mutations in PNKP are considered to be responsible for Microcephaly with seizures (MCSZ) and Ataxia-ocular motor apraxia 4 (AOA4).
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The data obtained suggest that PARP1 and TDP1 bind in an antiparallel orientation; the N-terminus of the former protein interacts with the C-terminal domain of the latter.
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Tyrosyl-DNA-phosphodiesterase I (TDP1) participates in the removal and repair of stabilized-Top2alpha cleavage complexes in human cells.
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varying expression levels of TOP1 and TDP1 polypeptides in multiple colorectal cancer cell lines and in clinical colorectal cancer samples, are reported.
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both TOP1 and TDP1 were upregulated in the tumor tissue compared to the adjacent non-tumor tissue in non-small cell lung cancer tissue
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Density functional theory computations are used to acquire thermodynamic and kinetic data along the catalytic pathway, including the phosphoryl transfers of Tdp1 and subsequent hydrolysis.
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TDP1 plays a role during the early stages of mammalian NHEJ. TPD1 stimulated DNA binding by XLF. TDP1 also promoted DNA binding by Ku70/80 and stimulated DNA-PK activity.
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These findings suggest that the flexibility of Tdp1 active site residues may impair the resolution of mutant Tdp1 covalent phosphohistidyl intermediates
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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
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TDP1 and APTX take part in the mitochondrial DNA repair and are apparently being transported from the cell nucleus. (Review)
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Data provides insights into the possible inactivation of TDP1 in cancers and its relationship to cellular response to Top1-targeted drugs.
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Results show Tdp1 catalyzes hydrolysis of apurinic/apyrimidinic site analog correlates with the DNA helix distortion induced by the substituent.
