UBR7 acts as a histone chaperone for post‐nucleosomal histone H3
Autor: | Alexander S. Lee, Ali Shilatifard, Daniel R. Foltz, Kyle P. Eagen, Justin Bodner, Alexander B. Willis, Celeste Rosencrance, Matthew N Gaynes, Ann K. Hogan, Shashank Srivastava, Aaron O. Bailey, Marc A. Morgan, Kizhakke M Sathyan, Jiehuan Huang, Sakshi Khurana, Ewelina Zasadzinska, Kelvin A. Wong |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
Ubiquitin-Protein Ligases
Nucleosomal histone Autoantigens General Biochemistry Genetics and Molecular Biology Cell Line Histones chemistry.chemical_compound Protein Domains Transcription (biology) Humans Molecular Biology General Immunology and Microbiology biology General Neuroscience Nuclear Proteins Articles Chromatin Cell biology Nucleosomes Histone Code Histone HEK293 Cells chemistry NASP Chaperone (protein) biology.protein H3K4me3 DNA HeLa Cells |
Zdroj: | EMBO J |
Popis: | Histone chaperones modulate the stability of histones beginning from histone synthesis, through incorporation into DNA, and during recycling during transcription and replication. Following histone removal from DNA, chaperones regulate histone storage and degradation. Here, we demonstrate that UBR7 is a histone H3.1 chaperone that modulates the supply of pre-existing post-nucleosomal histone complexes. We demonstrate that UBR7 binds to post-nucleosomal H3K4me3 and H3K9me3 histones via its UBR box and PHD. UBR7 binds to the non-nucleosomal histone chaperone NASP. In the absence of UBR7, the pool of NASP-bound post-nucleosomal histones accumulate and chromatin is depleted of H3K4me3-modified histones. We propose that the interaction of UBR7 with NASP and histones opposes the histone storage functions of NASP and that UBR7 promotes reincorporation of post-nucleosomal H3 complexes. |
Databáze: | OpenAIRE |
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