Proteomics

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BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures

ABSTRACT: We ran native 5% polyacrylamide-TBE gel for electro mobility shift assay (EMSA) for DNA/RNA G4 structures with or without recombinant human core-BLM (cBLM) protein, which was extracted and purified from E.coli in order to show binding of the RNA/DNA by this protein. To further evidence, we cut the equivalent gel area where the shifted band is located for all the wells (DNA only, DNA+cBLM, RNA, RNA+cBLM and cBLM only) and anlayzed by LC-MS/MS to identify human BLM and to see if there are some E.coli contaminations in those specific bands. Moreover, we analyzed the stock solution of the recombinant cBLM as general control.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Yehuda Danino  

LAB HEAD: Eran Hornstein

PROVIDER: PXD042983 | Pride | 2023-10-24

REPOSITORIES: pride

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Dataset's files

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Action DRS
HF1_EH_18737_DNA_30052023.msf Msf
HF1_EH_18737_DNA_30052023.raw Raw
HF1_EH_18737_DNA_cBLM_30052023.msf Msf
HF1_EH_18737_DNA_cBLM_30052023.raw Raw
HF1_EH_18737_RNA_30052023.msf Msf
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Publications

Bloom's syndrome (BLM) protein is a known nuclear helicase that is able to unwind DNA secondary structures such as G-quadruplexes (G4s). However, its role in the regulation of cytoplasmic processes that involve RNA G-quadruplexes (rG4s) has not been previously studied. Here, we demonstrate that BLM is recruited to stress granules (SGs), which are cytoplasmic biomolecular condensates composed of RNAs and RNA-binding proteins. BLM is enriched in SGs upon different stress conditions and in an rG4-d  ...[more]

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