SHPRH regulates rRNA transcription by recognizing the histone code in an mTOR-dependent manner

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) pr...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2017-04, Vol.114 (17), p.E3424-E3433
Main Authors: Lee, Deokjae, An, Jungeun, Park, Young-Un, Liaw, Hungjiun, Woodgate, Roger, Park, Jun Hong, Myung, Kyungjae
Format: Article
Language:English
Subjects:
Actinomycin
Biological Sciences
Cells
Deoxyribonucleic acid
DNA
DNA biosynthesis
DNA repair
DNA-directed RNA polymerase
Histone H3
Homeobox
Lysine
Nucleoli
PNAS Plus
Proliferating cell nuclear antigen
Proteins
Rapamycin
Repair
Ribonucleic acid
Ribosomal DNA
RNA
RNA polymerase
rRNA
Stalling
TOR protein
Transcription
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1701978114