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Molecular basis for DarT ADP-ribosylation of a DNA base
Structural and mechanistic data of the ADP-ribosyltransferase DarT demonstrate the role of ADP-ribosylation of DNA by this enzyme in generating toxicity and regulating cellular signalling processes in bacteria.
- Marion Schuller
- , Rachel E. Butler
- & Ivan Ahel
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Article |
Bridging of DNA breaks activates PARP2–HPF1 to modify chromatin
The PARP2–HPF1 histone-modifying complex bridges two nucleosomes to align broken DNA ends for ligation, initiating conformational changes that activate PARP2 and enable DNA damage repair.
- Silvija Bilokapic
- , Marcin J. Suskiewicz
- & Mario Halic
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News & Views |
A glimpse of molecular competition
Single-molecule studies reveal how the DNA-repair protein RecA overcomes competition from another protein to bind to single-stranded DNA, and how other mediator proteins assist in this process. See Letter p.274
- Susan T. Lovett
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Letter |
The yeast Fun30 and human SMARCAD1 chromatin remodellers promote DNA end resection
Fun30 and SMARCAD1 are identified as chromatin remodellers that promote DNA end resection during DNA repair and preserve genome stability in yeast and humans, respectively.
- Thomas Costelloe
- , Raphaël Louge
- & Bertrand Llorente
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Letter |
Bidirectional resection of DNA double-strand breaks by Mre11 and Exo1
- Valerie Garcia
- , Sarah E. L. Phelps
- & Matthew J. Neale
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Letter |
Crucial role for DNA ligase III in mitochondria but not in Xrcc1-dependent repair
Eukaryotic cells have several DNA ligases. DNA ligase III (Lig3) forms a complex with Xrcc1 that can function in nuclear repair. But, Lig3 null animals cannot be made; is this nuclear role in base excision repair its critical function? This is one of two papers showing that the role of Lig3 in the nucleus is non-essential. Rather, the catalytic activity of Lig3, but not Xrcc1, is essential for the maintenance of mitochondria.
- Deniz Simsek
- , Amy Furda
- & Maria Jasin
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Letter |
Iron-catalysed oxidation intermediates captured in a DNA repair dioxygenase
Mononuclear iron-containing oxygenases have many important roles in the cell, including the demethylation of DNA and histones. These authors crystallized the AlkB oxygenase in complex with various modified DNAs. By growing the crystals under anaerobic conditions and then exposing them to dioxygen to initiate oxidation, two different intermediates were trapped. A third type of intermediate was determined using additional computational analysis. These structures provide insight into how these enzymes perform oxidative demethylation.
- Chengqi Yi
- , Guifang Jia
- & Chuan He
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Letter |
Telomeres avoid end detection by severing the checkpoint signal transduction pathway
The ends of chromosomes, known as telomeres, look like ends generated by double-strand breaks, but if treated as such the DNA damage repair system would initiate a checkpoint response and cause telomere–telomere fusions. These authors show that telomeres lack two types of histone modification that are required for recruitment of Crb2b53BP1, without which the checkpoint cannot be activated even if other DNA damage response proteins are recruited to a Taz1-deficient telomere.
- Tiago Carneiro
- , Lyne Khair
- & Miguel Godinho Ferreira
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Letter |
Dynamics and mechanism of repair of ultraviolet-induced (6–4) photoproduct by photolyase
The repair enzyme (6–4) photolyase uses light energy to cleave the ultraviolet-induced bond between pyrimidine dimers. These authors use ultrafast spectroscopy to examine the detailed electron and proton movements during the catalytic photocycle. Histidine 364 is identified as the crucial residue involved in the rate-limiting step.
- Jiang Li
- , Zheyun Liu
- & Dongping Zhong
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News & Views |
How to accurately bypass damage
Ultraviolet radiation can cause cancer through DNA damage — specifically, by linking adjacent thymine bases. Crystal structures show how the enzyme DNA polymerase η accurately bypasses such lesions, offering protection.
- Suse Broyde
- & Dinshaw J. Patel