m 6 A modification of HSATIII lncRNAs regulates temperature‐dependent splicing
| Autor: | Kensuke Ninomiya, Goro Terai, Kiyoshi Asai, Mahmoud Khamis Aly, Tohru Natsume, Tetsuro Hirose, Yuriko Sakaguchi, Junichi Iwakiri, Tsutomu Suzuki, Shungo Adachi |
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| Rok vydání: | 2021 |
| Předmět: |
Adenosine
RNA Splicing Nerve Tissue Proteins Protein Serine-Threonine Kinases Biology General Biochemistry Genetics and Molecular Biology CLK1 03 medical and health sciences 0302 clinical medicine Humans RNA Messenger Phosphorylation Molecular Biology Psychological repression Repetitive Sequences Nucleic Acid 030304 developmental biology Ribonucleoprotein Cell Nucleus 0303 health sciences Nucleoplasm Serine-Arginine Splicing Factors General Immunology and Microbiology General Neuroscience Temperature Intron Articles Protein-Tyrosine Kinases Long non-coding RNA Cell biology RNA splicing RNA Long Noncoding RNA Splicing Factors 030217 neurology & neurosurgery HeLa Cells |
| Zdroj: | EMBO J |
| ISSN: | 1460-2075 0261-4189 |
| Popis: | Nuclear stress bodies (nSBs) are nuclear membraneless organelles formed around stress‐inducible HSATIII architectural long noncoding RNAs (lncRNAs). nSBs repress splicing of hundreds of introns during thermal stress recovery, which are partly regulated by CLK1 kinase phosphorylation of temperature‐dependent Ser/Arg‐rich splicing factors (SRSFs). Here, we report a distinct mechanism for this splicing repression through protein sequestration by nSBs. Comprehensive identification of RNA‐binding proteins revealed HSATIII association with proteins related to N(6)‐methyladenosine (m(6)A) RNA modification. 11% of the first adenosine in the repetitive HSATIII sequence were m(6)A‐modified. nSBs sequester the m(6)A writer complex to methylate HSATIII, leading to subsequent sequestration of the nuclear m(6)A reader, YTHDC1. Sequestration of these factors from the nucleoplasm represses m(6)A modification of pre‐mRNAs, leading to repression of m(6)A‐dependent splicing during stress recovery phase. Thus, nSBs serve as a common platform for regulation of temperature‐dependent splicing through dual mechanisms employing two distinct ribonucleoprotein modules with partially m(6)A‐modified architectural lncRNAs. |
| Databáze: | OpenAIRE |
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