ArticleScientific reports2013
Structure of the RecQ C-terminal domain of human Bloom syndrome protein.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 23 citations in OpenAlex.
- Shuttling of RecQ helicase HIM-6 coordinates iterative cycle of unwinding, pulling, and backsliding.Nucleic acids research · 2026Article
- Review
- Response to Replication Stress and Maintenance of Genome Stability by WRN, the Werner Syndrome Protein.International journal of molecular sciences · 2024Review
- Biochemical Properties of Naturally Occurring Human Bloom Helicase Variants.bioRxiv : the preprint server for biology · 2023Article
- Interaction landscape of a 'CRSC advances · 2019Article
- RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions.Nature communications · 2018Article
- The Biology of Aging and Cancer: A Brief Overview of Shared and Divergent Molecular Hallmarks.Aging and disease · 2017Review
- Bloom's syndrome: Why not premature aging?: A comparison of the BLM and WRN helicases.Ageing research reviews · 2017Review
- Bloom's Syndrome: Clinical Spectrum, Molecular Pathogenesis, and Cancer Predisposition.Molecular syndromology · 2017Review
- Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes.Nucleic acids research · 2015Article
- Unwinding forward and sliding back: an intermittent unwinding mode of the BLM helicase.Nucleic acids research · 2015Article
- Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures.Nature communications · 2014Article
- Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein.Journal of biomolecular NMR · 2014Article
- Structural mechanisms of human RecQ helicases WRN and BLM.Frontiers in genetics · 2014Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bloom syndrome is a rare genetic disorder characterized by genomic instability and cancer predisposition. The disease is caused by mutations of the Bloom syndrome protein (BLM). Here we report the crystal structure of a RecQ C-terminal (RQC) domain from human BLM. The structure reveals three novel features of BLM RQC which distinguish it from the previous structures of the Werner syndrome protein (WRN) and RECQ1. First, BLM RQC lacks an aromatic residue at the tip of the β-wing, a key element of the RecQ-family helicases used for DNA-strand separation. Second, a BLM-specific insertion between the N-terminal helices exhibits a looping-out structure that extends at right angles to the β-wing. Deletion mutagenesis of this insertion interfered with binding to Holliday junction. Third, the C-terminal region of BLM RQC adopts an extended structure running along the domain surface, which may facilitate the spatial positioning of an HRDC domain in the full-length protein.
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