ArticleProceedings of the National Academy of Sciences of the United States of America2014
CRL4-like Clr4 complex in Schizosaccharomyces pombe depends on an exposed surface of Dos1 for heterochromatin silencing.
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. An erratum has been issued. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
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- A periplasmic protein complex mediates arabinofuranosyltransferase activity and intrinsic drug resistance inScience advances · 2026Article
- An H3K14ub-H3K9me3 feedback circuit governs heterochromatin spreading and inheritance in fission yeast.Nature communications · 2026Article
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- Clr4Nature communications · 2024Article
- Heterochromatin repeat organization at an individual level: Rex1BD and the 14-3-3 protein coordinate to shape the epigenetic landscape within heterochromatin repeats.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024Review
- The Cross-Regulation Between Set1, Clr4, and Lsd1/2 in Schizosaccharomyces pombe.PLoS genetics · 2024Article
- Telomere-to-Telomere genome assemblies of human-infecting Encephalitozoon species.BMC genomics · 2023Article
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- Post-Translational Modifications of Histones Are Versatile Regulators of Fungal Development and Secondary Metabolism.Toxins · 2022Review
- Breakers and amplifiers in chromatin circuitry: acetylation and ubiquitination control the heterochromatin machinery.Current opinion in structural biology · 2021Review
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- Limited DNA Repair Gene Repertoire in Ascomycete Yeast Revealed by Comparative Genomics.Genome biology and evolution · 2019Article
- H3K14 ubiquitylation promotes H3K9 methylation for heterochromatin assembly.EMBO reports · 2019Article
- Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity.Nucleic acids research · 2019Article
- Induction of H3K9me3 and DNA methylation by tethered heterochromatin factors inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- DNA replication components as regulators of epigenetic inheritance--lesson from fission yeast centromere.Protein & cell · 2014Review
- A systematic genetic screen identifies new factors influencing centromeric heterochromatin integrity in fission yeast.Genome biology · 2014Article
- The RFTS domain of Raf2 is required for Cul4 interaction and heterochromatin integrity in fission yeast.PloS one · 2014Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Repressive histone H3 lysine 9 methylation (H3K9me) and its recognition by HP1 proteins are necessary for pericentromeric heterochromatin formation. In Schizosaccharomyces pombe, H3K9me deposition depends on the RNAi pathway. Cryptic loci regulator 4 (Clr4), the only known H3K9 methyltransferase in this organism, is a subunit of the Clr4 methyltransferase complex (CLRC), whose composition is reminiscent of a CRL4 type cullin-RING ubiquitin ligase (CRL) including its cullin Cul4, the RING-box protein Pip1, the DNA damage binding protein 1 homolog Rik1, and the DCAF-like protein delocalization of Swi6 1 (Dos1). Dos2 and Stc1 have been proposed to be part of the complex but do not bear similarity to canonical ubiquitin ligase components. CLRC is an active E3 ligase in vitro, and this activity is necessary for heterochromatin assembly in vivo. The similarity between CLRC and the CRLs suggests that the WD repeat protein Dos1 will act to mediate target recognition and substrate specificity for CLRC. Here, we present a pairwise interaction screen that confirms a CRL4-like subunit arrangement and further identifies Dos2 as a central component of the complex and recruiter of Stc1. We determined the crystal structure of the Dos1 WD repeat domain, revealing an eight-bladed β-propeller fold. Functional mapping of the putative target-binding surface of Dos1 identifies key residues required for heterochromatic silencing, consistent with Dos1's role as the specificity factor for the E3 ubiquitin ligase.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.