ArticleProceedings of the National Academy of Sciences of the United States of America2014
A structure-specific nucleic acid-binding domain conserved among DNA repair proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 44 citations in OpenAlex.
- FBH1 Reverses Stalled Replication Forks via Sequential Unwinding of Nascent Strands.bioRxiv : the preprint server for biology · 2026Article
- Structural basis for fork reversal and RAD51 regulation by the SCF ubiquitin ligase complex of F-box helicase 1.Nature communications · 2026Article
- Information theory optimization of signals from small-angle scattering measurements.Biophysical journal · 2025Article
- Mechanisms and regulation of replication fork reversal.DNA repair · 2024Review
- Repair and tolerance of DNA damage at the replication fork: A structural perspective.Current opinion in structural biology · 2023Review
- RAD51 bypasses the CMG helicase to promote replication fork reversal.Science (New York, N.Y.) · 2023Article
- Time for remodeling: SNF2-family DNA translocases in replication fork metabolism and human disease.DNA repair · 2020Review
- The DNA repair protein SHPRH is a nucleosome-stimulated ATPase and a nucleosome-E3 ubiquitin ligase.Epigenetics & chromatin · 2019Article
- Transcription preinitiation complex structure and dynamics provide insight into genetic diseases.Nature structural & molecular biology · 2019Article
- Article
- In vitro reconstitution of DNA replication initiated by genetic recombination: a T4 bacteriophage model for a type of DNA synthesis important for all cells.Molecular biology of the cell · 2019Article
- Movement of the RecG Motor Domain upon DNA Binding Is Required for Efficient Fork Reversal.International journal of molecular sciences · 2018Article
- The HIRAN domain of helicase-like transcription factor positions the DNA translocase motor to drive efficient DNA fork regression.The Journal of biological chemistry · 2018Article
- The phage T4 MotA transcription factor contains a novel DNA binding motif that specifically recognizes modified DNA.Nucleic acids research · 2018Article
- RPA and RAD51: fork reversal, fork protection, and genome stability.Nature structural & molecular biology · 2018Review
- Functions of SMARCAL1, ZRANB3, and HLTF in maintaining genome stability.Critical reviews in biochemistry and molecular biology · 2017Review
- Replication fork regression and its regulation.FEMS yeast research · 2017Review
- SAXS studies of RNA: structures, dynamics, and interactions with partners.Wiley interdisciplinary reviews. RNA · 2016Review
- Identification of a Substrate Recognition Domain in the Replication Stress Response Protein Zinc Finger Ran-binding Domain-containing Protein 3 (ZRANB3).The Journal of biological chemistry · 2016Article
- Human HLTF mediates postreplication repair by its HIRAN domain-dependent replication fork remodelling.Nucleic acids research · 2015Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
SMARCAL1, a DNA remodeling protein fundamental to genome integrity during replication, is the only gene associated with the developmental disorder Schimke immuno-osseous dysplasia (SIOD). SMARCAL1-deficient cells show collapsed replication forks, S-phase cell cycle arrest, increased chromosomal breaks, hypersensitivity to genotoxic agents, and chromosomal instability. The SMARCAL1 catalytic domain (SMARCAL1(CD)) is composed of an SNF2-type double-stranded DNA motor ATPase fused to a HARP domain of unknown function. The mechanisms by which SMARCAL1 and other DNA translocases repair replication forks are poorly understood, in part because of a lack of structural information on the domains outside of the common ATPase motor. In the present work, we determined the crystal structure of the SMARCAL1 HARP domain and examined its conformation and assembly in solution by small angle X-ray scattering. We report that this domain is conserved with the DNA mismatch and damage recognition domains of MutS/MSH and NER helicase XPB, respectively, as well as with the putative DNA specificity motif of the T4 phage fork regression protein UvsW. Loss of UvsW fork regression activity by deletion of this domain was rescued by its replacement with HARP, establishing the importance of this domain in UvsW and demonstrating a functional complementarity between these structurally homologous domains. Mutation of predicted DNA-binding residues in HARP dramatically reduced fork binding and regression activities of SMARCAL1(CD). Thus, this work has uncovered a conserved substrate recognition domain in DNA repair enzymes that couples ATP-hydrolysis to remodeling of a variety of DNA structures, and provides insight into this domain's role in replication fork stability and genome integrity.
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