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Journal article
RNase P protein subunit Rpp29 represses histone H3.3 nucleosome deposition
Molecular biology of the cell, v 27(7), pp 1154-1169
01 Apr 2016
PMID: 26842893
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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.
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Details
- Title
- RNase P protein subunit Rpp29 represses histone H3.3 nucleosome deposition
- Creators
- Alyshia Newhart - The Wistar InstituteSara Lawrence Powers - The Wistar InstitutePrashanth Krishna Shastrula - The Wistar InstituteIsabel Sierra - The Wistar InstituteLucy M Joo - The Wistar InstituteJames E Hayden - The Wistar InstituteAndrew R Cohen - Drexel UniversitySusan M Janicki - The Wistar Institute
- Publication Details
- Molecular biology of the cell, v 27(7), pp 1154-1169
- Grant note
- R01 GM 093000-02 / NIGMS NIH HHS P30 CA010815 / NCI NIH HHS P30 CA10815 / NCI NIH HHS R01 GM093000 / NIGMS NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Electrical and Computer Engineering
- Web of Science ID
- WOS:000372971100009
- Scopus ID
- 2-s2.0-84962368299
- Other Identifier
- 991019169659804721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Cell Biology