ArticleJournal of molecular biology2015
An ATPase-deficient variant of the SNF2 family member HELLS shows altered dynamics at pericentromeric heterochromatin.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 14 citations in OpenAlex.
- Severe Ecthyma Gangrenosum in a Pediatric Patient With Neutropenia and a Novel HELLS Variant: Case Report.Clinical case reports · 2026Article
- Hells protects mitochondrial integrity via Nr2f2 suppression during osteoclast differentiation.Cell communication and signaling : CCS · 2026Article
- Article
- Chromatin remodeling of histone H3 variants underlies epigenetic inheritance of DNA methylation.bioRxiv : the preprint server for biology · 2023Article
- The Molecular Pathogenesis of Tumor-SuppressiveCells · 2023Article
- Seminars in cell and development biology on histone variants remodelers of H2A variants associated with heterochromatin.Seminars in cell & developmental biology · 2023Review
- Regulation of Oncogenic Targets by Tumor-SuppressiveBiomedicines · 2021Article
- The Significance of HOXC11 and LSH in Survival Prediction in Gastric Adenocarcinoma.OncoTargets and therapy · 2021Article
- Article
- Article
- Lsh/HELLS is required for B lymphocyte development and immunoglobulin class switch recombination.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Chromatin condensation fluctuations rather than steady-state predict chromatin accessibility.Nucleic acids research · 2019Article
- The chromatin remodeling protein Lsh alters nucleosome occupancy at putative enhancers and modulates binding of lineage specific transcription factors.Epigenetics · 2019Article
- Review
- The SNF2 family ATPase LSH promotes cell-autonomous de novo DNA methylation in somatic cells.Nucleic acids research · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The HELLS (helicase, lymphoid specific, also known as lymphoid-specific helicase) protein is related to the SNF2 (sucrose non-fermentable 2) family of chromatin remodeling ATPases. It is required for efficient DNA methylation in mammals, particularly at heterochromatin-located repetitive sequences. In this study, we investigated the interaction of HELLS with chromatin and used an ATPase-deficient HELLS variant to address the role of ATP hydrolysis in this process. Chromatin fractionation experiments demonstrated that, in the absence of the ATPase activity, HELLS is retained at the nuclear matrix compartment, defined in part by lamin B1. Microscopy studies revealed a stronger association of the ATPase-deficient mutant with heterochromatin. These results were further supported by fluorescence recovery after photobleaching measurements, which showed that, at heterochromatic sites, wild-type HELLS is very dynamic, with a recovery half-time of 0.8s and a mobile protein fraction of 61%. In contrast, the ATPase-deficient mutant displayed 4.5-s recovery half-time and a reduction in the mobile fraction to 30%. We also present evidence suggesting that, in addition to the ATPase activity, a functional H3K9me3 signaling pathway contributes to an efficient release of HELLS from pericentromeric chromatin. Overall, our results show that a functional ATPase activity is not required for the recruitment of HELLS to heterochromatin, but it is important for the release of the enzyme from these sites.
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Registered trials
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