The Cullin-4 Complex DCDC Does Not Require E3 Ubiquitin Ligase Elements To Control Heterochromatin in Neurospora crassa
| Autor: | Zachary A. Lewis, Eric U. Selker, Jordan D Gessaman, Paula L. Grisafi, Shinji Honda, Keyur K. Adhvaryu |
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| Rok vydání: | 2015 |
| Předmět: |
Heterochromatin
Ubiquitin-Protein Ligases Microbiology NEDD8 Fungal Proteins DDB1 Non-histone protein Ubiquitins Molecular Biology chemistry.chemical_classification DNA ligase Neurospora crassa biology fungi EZH2 Articles General Medicine DNA Methylation Cullin Proteins Protein Structure Tertiary Ubiquitin ligase Biochemistry chemistry biology.protein Cullin Protein Binding Transcription Factors |
| Zdroj: | Eukaryotic Cell. 14:25-28 |
| ISSN: | 1535-9786 1535-9778 |
| DOI: | 10.1128/ec.00212-14 |
| Popis: | The cullin-4 (CUL4) complex DCDC ( D IM-5/-7/-9/ C UL4/ D DB1 c omplex) 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. |
| Databáze: | OpenAIRE |
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