RNase P protein subunit Rpp29 represses histone H3.3 nucleosome deposition
| Autor: | Alyshia Newhart, Susan M. Janicki, James Hayden, Lucy M. Joo, Sara Lawrence Powers, Prashanth Krishna Shastrula, Isabel Sierra, Andrew R. Cohen |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Euchromatin Chromosomal Proteins Non-Histone RNase P Heterochromatin Epigenesis Genetic Histones 03 medical and health sciences Histone H3 Ribonucleases 0302 clinical medicine Humans Histone code Nucleosome Molecular Biology biology Nuclear Functions Articles Cell Biology Chromatin Assembly and Disassembly Molecular biology Nucleosomes Chromatin 030104 developmental biology Histone Ribonucleoproteins biology.protein 030217 neurology & neurosurgery |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.e15-02-0099 |
| Popis: | RNase P protein subunits Rpp29, POP1, and Rpp21 interact with histone H3.3 upstream of nucleosome deposition, suggesting that a variant of this enzyme regulates H3.3 function. Rpp29 knockdown increases H3.3 chromatin incorporation, suggesting that it represses H3.3 nucleosome deposition, which has important implications for epigenetic regulation. In mammals, histone H3.3 is a critical regulator of transcription state change and heritability at both euchromatin and heterochromatin. The H3.3-specific chaperone, DAXX, together with the chromatin-remodeling factor, ATRX, regulates H3.3 deposition and transcriptional silencing at repetitive DNA, including pericentromeres and telomeres. However, the events that precede H3.3 nucleosome incorporation have not been fully elucidated. We previously showed that the DAXX-ATRX-H3.3 pathway regulates a multi-copy array of an inducible transgene that can be visualized in single living cells. When this pathway is impaired, the array can be robustly activated. H3.3 is strongly recruited to the site during activation where it accumulates in a complex with transcribed sense and antisense RNA, which is distinct from the DNA/chromatin. This suggests that transcriptional events regulate H3.3 recruited to its incorporation sites. Here we report that the nucleolar RNA proteins Rpp29, fibrillarin, and RPL23a are also components of this H3.3/RNA complex. Rpp29 is a protein subunit of RNase P. Of the other subunits, POP1 and Rpp21 are similarly recruited suggesting that a variant of RNase P regulates H3.3 chromatin assembly. Rpp29 knockdown increases H3.3 chromatin incorporation, which suggests that Rpp29 represses H3.3 nucleosome deposition, a finding with implications for epigenetic regulation. |
| Databáze: | OpenAIRE |
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