ArticleEukaryotic cell2015
The cullin-4 complex DCDC does not require E3 ubiquitin ligase elements to control heterochromatin in Neurospora crassa.
Article in Eukaryotic cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 12 citations in OpenAlex.
- Review
- Article
- Evolutionary Variation in MADS Box Dimerization Affects Floral Development and Protein Abundance in Maize.The Plant cell · 2020Article
- Limited DNA Repair Gene Repertoire in Ascomycete Yeast Revealed by Comparative Genomics.Genome biology and evolution · 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
- Neurospora chromosomes are organized by blocks of importin alpha-dependent heterochromatin that are largely independent of H3K9me3.Genome research · 2016Article
- Genome-wide redistribution of H3K27me3 is linked to genotoxic stress and defective growth.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Neurospora importin α is required for normal heterochromatic formation and DNA methylation.PLoS genetics · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The cullin-4 (CUL4) complex DCDC (DIM-5/-7/-9/CUL4/DDB1 complex) is essential for DNA methylation and heterochromatin formation in Neurospora crassa. Cullins form the scaffold of cullin-RING E3 ubiquitin ligases (CRLs) and are modified by the covalent attachment of NEDD8, a ubiquitin-like protein that regulates the stability and activity of CRLs. We report that neddylation is not required for CUL4-dependent DNA methylation or heterochromatin formation but is required for the DNA repair functions. Moreover, the RING domain protein RBX1 and a segment of the CUL4 C terminus that normally interacts with RBX1, the E2 ligase, CAND1, and CSN are dispensable for DNA methylation and heterochromatin formation by DCDC. Our study provides evidence for the noncanonical functions of core CRL components.
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