Instability and decay of the primary structure of DNA
- T. Lindahl
- Biology, ChemistryNature
- 22 April 1993
The spontaneous decay of DNA is likely to be a major factor in mutagenesis, carcinogenesis and ageing, and also sets limits for the recovery of DNA fragments from fossils.
N6-Methyladenosine in Nuclear RNA is a Major Substrate of the Obesity-Associated FTO
FTO exhibits efficient oxidative demethylation activity of abundant N6-methyladenosine (m6A) residues in RNA in vitro, and it is shown that FTO partially colocalizes with nuclear speckles, supporting m6A in nuclear RNA as a physiological substrate of FTO.
Immunoglobulin Isotype Switching Is Inhibited and Somatic Hypermutation Perturbed in UNG-Deficient Mice
The Obesity-Associated FTO Gene Encodes a 2-Oxoglutarate-Dependent Nucleic Acid Demethylase
It is found that recombinant murine Fto catalyzes the Fe(II)- and 2OG-dependent demethylation of 3-methylthymine in single-stranded DNA, with concomitant production of succinate, formaldehyde, and carbon dioxide.
Human DNA Repair Genes
Modulation of DNA repair should lead to clinical applications including improvement of radiotherapy and treatment with anticancer drugs and an advanced understanding of the cellular aging process.
Mutations in the gene encoding the 3′-5′ DNA exonuclease TREX1 cause Aicardi-Goutières syndrome at the AGS1 locus
TREX1, encoding the major mammalian 3′ → 5′ DNA exonuclease, is the AGS1 gene, and AGS-causing mutations result in abrogation of TREX1 enzyme activity, and failure of which results in the triggering of an abnormal innate immune response.
Reconstitution of DNA base excision‐repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein.
- Y. Kubota, R. Nash, A. Klungland, P. Schär, D. Barnes, T. Lindahl
- Biology, ChemistryEMBO Journal
- 1 December 1996
Data indicate that XRCC1, which has no known catalytic activity, might serve as a scaffold protein during base excision‐repair, allowing for more efficient ligation after filling of a single nucleotide patch.
Second pathway for completion of human DNA base excision‐repair: reconstitution with purified proteins and requirement for DNase IV (FEN1)
The structure‐specific nuclease DNase IV (FEN1) was essential for repair of a reduced AP site, which occurred through the long‐patch BER pathway, which was largely dependent on DNA polymerase β in cell extracts, but the reaction could be reconstituted with either DNA polymerases β or δ.
Rate of depurination of native deoxyribonucleic acid.