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SHPRH regulates rRNA transcription by recognizing the histone code in an mTOR-dependent manner.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2017 Apr 25; Vol. 114 (17), pp. E3424-E3433. Date of Electronic Publication: 2017 Apr 11. - Publication Year :
- 2017
-
Abstract
- Many DNA repair proteins have additional functions other than their roles in DNA repair. In addition to catalyzing PCNA polyubiquitylation in response to the stalling of DNA replication, SHPRH has the additional function of facilitating rRNA transcription by localizing to the ribosomal DNA (rDNA) promoter in the nucleoli. SHPRH was recruited to the rDNA promoter using its plant homeodomain (PHD), which interacts with histone H3 when the fourth lysine of H3 is not trimethylated. SHPRH enrichment at the rDNA promoter was inhibited by cell starvation, by treatment with actinomycin D or rapamycin, or by depletion of CHD4. SHPRH also physically interacted with the RNA polymerase I complex. Taken together, we provide evidence that SHPRH functions in rRNA transcription through its interaction with histone H3 in a mammalian target of rapamycin (mTOR)-dependent manner.<br />Competing Interests: The authors declare no conflict of interest.
- Subjects :
- DNA Helicases genetics
Gene Deletion
HeLa Cells
Histones genetics
Humans
Methylation
Mi-2 Nucleosome Remodeling and Deacetylase Complex genetics
Mi-2 Nucleosome Remodeling and Deacetylase Complex metabolism
RNA, Ribosomal genetics
TOR Serine-Threonine Kinases genetics
Ubiquitin-Protein Ligases genetics
DNA Helicases metabolism
Histones metabolism
Promoter Regions, Genetic
RNA, Ribosomal biosynthesis
TOR Serine-Threonine Kinases metabolism
Transcription, Genetic
Ubiquitin-Protein Ligases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1091-6490
- Volume :
- 114
- Issue :
- 17
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 28400511
- Full Text :
- https://doi.org/10.1073/pnas.1701978114