Mutational phospho-mimicry reveals a regulatory role for the XRCC4 and XLF C-terminal tails in modulating DNA bridging during classical non-homologous end joining

XRCC4 and DNA Ligase 4 (LIG4) form a tight complex that provides DNA ligase activity for classical non-homologous end joining (the predominant DNA double-strand break repair pathway in higher eukaryotes) and is stimulated by XLF. Independently of LIG4, XLF also associates with XRCC4 to form filament...

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Vydané v:	eLife Ročník 6
Hlavní autori:	Normanno, Davide, Négrel, Aurélie, de Melo, Abinadabe J, Betzi, Stéphane, Meek, Katheryn, Modesti, Mauro
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	England eLife Sciences Publications Ltd 13.05.2017 eLife Sciences Publication eLife Sciences Publications, Ltd
Predmet:	Alanine Amino Acid Substitution Biochemistry Deoxyribonucleic acid DNA DNA - metabolism DNA damage DNA End-Joining Repair DNA Mutational Analysis DNA repair DNA Repair Enzymes - genetics DNA Repair Enzymes - metabolism DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism DNA-dependent protein kinase Double-strand break repair Filaments Genes and Chromosomes Humans Kinases Life Sciences LIG4 protein Mimicry Mutation NHEJ Non-homologous end joining Phosphorylation Plasmids Protein Binding Protein Processing, Post-Translational XLF XRCC4 XLF XRCC4 genes biochemistry chromosomes NHEJ human
ISSN:	2050-084X, 2050-084X
On-line prístup:	Získať plný text
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