Dataset Information

Role of PRMT5 in DNA damage response

ABSTRACT: Protein arginine methyltransferase (PRMT5) has emerged as a crucial symmetric dimethylating enzyme involved in the methylation of a myriad of substrates critical for epigenetic regulation, DNA damage signalling, RNA splicing, and cell fate decision. Here we have uploaded the PRMT5 interactome with the nuclear and mitochondrial proteins. The Arginine methylation of rge proteins were evaluated for biological Function.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hek-293 Cell

SUBMITTER: Benu Brata Das

LAB HEAD: Benu Brata

PROVIDER: PXD057645 | Pride | 2026-03-16

REPOSITORIES: Pride

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Publications

PRMT5 in mitochondria regulates mtDNA stability through TFAM arginine methylation.

Bhattacharjee Sangheeta S Das Sayan S Chowdhury Banhi B Das Benu Brata BB

Nature communications 20260223 1

Protein arginine methyltransferase 5 (PRMT5) catalyzes arginine methylation and regulates cellular functions such as proliferation, RNA splicing, and nuclear DNA damage response. This study uncovers that a fraction of nuclear-encoded PRMT5 localizes to the mitochondria, which is critical for maintaining mitochondrial DNA (mtDNA) homeostasis. PRMT5 knockout (PRMT5<sup>-/-</sup>) cells had reduced nucleoid counts, diminished mtDNA copy numbers, disrupted the balance of the mitochondrial fission-fu ...[more]

PMID: 41730877

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Project description:The protein arginine methyl transferase PRMT5 is an enzyme expressed in oligodendrocyte lineage cells and responsible for the symmetric methylation of arginine residues on histone tails. Previous work from our laboratory identified PRMT5 as critical for myelination, due to its transcriptional regulation of survival and early stages of differentiation. However, besides its nuclear localization, PRMT5 is found at high levels in the cytoplasm of oligodendrocyte progenitor cells (OPCs) and yet, its interacting partners and non-histone substrates in this lineage, remain elusive. By using mass spectrometry on protein eluates from extracts generated from OPC and immunoprecipitated with PRMT5 antibodies, we identified 1116 proteins as PRMT5 interacting partners. These proteins are related to molecular functions such as RNA binding, ribosomal structure, nucleotide binding, cadherin and actin binding, GTP and GTPase activity. We then investigated PRMT5 substrates using iTRAQ-based proteomics on protein samples isolated from CRISPR-PRMT5 knockdown immortalized oligodendrocyte progenitors compared to CRISPR-EGFP controls. This analysis identified 169 peptides with statistically different symmetric methylation of arginine residues in the two groups. Those peptides led to 30 unique non-histone substrates of PRMT5. The majority of these proteins were consistent with PRMT5 substrates, previously identified in distinct cancer cell lines (e.g. the transcription factor ZN326), and were functionally related to RNA processing and transport, splicing, regulation of mRNA stability and transcription. In addition, we detected three substrates as unique to the oligodendrocyte lineage and not identified in cancer cells. They included the proline-rich protein PRC2C, involved in methyl-RNA binding, the RNA binding protein KHDR2, regulating splicing events and the heterogeneous nuclear RNA binding protein HNRPD, involved in regulation of RNA stability. Together, these results highlight a cell-specific role of PRMT5 in regulating, not only transcription, but RNA processing and translation in OPCs. (287 WORDS)

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Dataset Information

Role of PRMT5 in DNA damage response

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Publications

PRMT5 in mitochondria regulates mtDNA stability through TFAM arginine methylation.

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