ArticleJournal of structural biology2010
The bridge-region of the Ku superfamily is an atypical zinc ribbon domain.
Article in Journal of structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Systematic evaluation of the DNA repair machinery facilitated the development of efficient genome editing tools for the red yeastSynthetic and systems biotechnology · 2027Article
- Structural basis for the inactivation of cytosolic DNA sensing by the vaccinia virus.Nature communications · 2022Article
- Proteomics of Salt Gland-Secreted Sap Indicates a Pivotal Role for Vesicle Transport and Energy Metabolism in Plant Salt Secretion.International journal of molecular sciences · 2022Article
- HMCES Functions in the Alternative End-Joining Pathway of the DNA DSB Repair during Class Switch Recombination in B Cells.Molecular cell · 2020Article
- Evolutionary convergence and divergence in archaeal chromosomal proteins and Chromo-like domains from bacteria and eukaryotes.Scientific reports · 2018Article
- Homo- and Heterodimerization of Proteins in Cell Signaling: Inhibition and Drug Design.Advances in protein chemistry and structural biology · 2018Review
- VCP/p97 Extracts Sterically Trapped Ku70/80 Rings from DNA in Double-Strand Break Repair.Molecular cell · 2016Article
- Phosphorylation of Ku dictates DNA double-strand break (DSB) repair pathway choice in S phase.Nucleic acids research · 2016Article
- The UBR-box and its relationship to binuclear RING-like treble clef zinc fingers.Biology direct · 2015Article
- A moonlighting function of Mycobacterium smegmatis Ku in zinc homeostasis?Protein science : a publication of the Protein Society · 2015Article
- Functional diversification of the RING finger and other binuclear treble clef domains in prokaryotes and the early evolution of the ubiquitin system.Molecular bioSystems · 2011Article
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Authors and funding
2 authors at 2 institutions in 1 country.
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Abstract
Members of the Ku superfamily are DNA-end-binding proteins involved in non-homologous end-joining (NHEJ) DNA repair. The published crystal structure of human Ku-DNA complex reveals a heterodimer that forms a ring around dsDNA by means of the Ku core modules. These modules contain a highly conserved seven-stranded β-barrel, which in turn contains an insertion, termed the bridge-region, between its second and third β-strands. The bridge-region adopts an unusual β-strand-rich structure critical for dsDNA-binding and Ku function, but its provenance remains unclear. Here, we demonstrate that the bridge-region of Ku is a novel member of the diverse Zn-ribbon fold group. Sequence analysis reveals that Ku from several Gram-positive bacteria and bacteriophages retain metal-chelating motifs, whereas they have been lost in the versions from most other organisms. Structural comparisons suggest that the Zn-ribbon from Ku-bridge-region is the first example of a circularly permuted, segment-swapped Zn-ribbon. This finding helps explain how Ku is likely to bind DNA as an obligate dimer. Further, we hypothesize that retention of the unusual conformation of the turns of the Zn-ribbons, despite loss of the Zn-binding sites, provides clues regarding the mechanism by which the Ku-bridge-regions sense the DNA state.
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