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Low complexity RGG-motif sequence is required for Processing body (P-body) disassembly

Author

Listed:
  • Raju Roy

    (Indian Institute of Science)

  • Gitartha Das

    (Indian Institute of Science)

  • Ishwarya Achappa Kuttanda

    (Indian Institute of Science)

  • Nupur Bhatter

    (Indian Institute of Science)

  • Purusharth I. Rajyaguru

    (Indian Institute of Science)

Abstract

P-bodies are conserved mRNP complexes that are implicated in determining mRNA fate by affecting translation and mRNA decay. In this report, we identify RGG-motif containing translation repressor protein Sbp1 as a disassembly factor of P-bodies since disassembly of P-bodies is defective in Δsbp1. RGG-motif is necessary and sufficient to rescue the PB disassembly defect in Δsbp1. Binding studies using purified proteins revealed that Sbp1 physically interacts with Edc3 and Sbp1-Edc3 interaction competes with Edc3-Edc3 interaction. Purified Edc3 forms assemblies, promoted by the presence of RNA and NADH and the addition of purified Sbp1, but not the RGG-deletion mutant, leads to significantly decreased Edc3 assemblies. We further note that the aggregates of human EWSR1 protein, implicated in neurodegeneration, are more persistent in the absence of Sbp1 and overexpression of EWSR1 in Δsbp1 leads to a growth defect. Taken together, our observations suggest a role of Sbp1 in disassembly, which could apply to disease-relevant heterologous protein-aggregates.

Suggested Citation

  • Raju Roy & Gitartha Das & Ishwarya Achappa Kuttanda & Nupur Bhatter & Purusharth I. Rajyaguru, 2022. "Low complexity RGG-motif sequence is required for Processing body (P-body) disassembly," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29715-5
    DOI: 10.1038/s41467-022-29715-5
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    1. Hong Joo Kim & Nam Chul Kim & Yong-Dong Wang & Emily A. Scarborough & Jennifer Moore & Zamia Diaz & Kyle S. MacLea & Brian Freibaum & Songqing Li & Amandine Molliex & Anderson P. Kanagaraj & Robert Ca, 2013. "Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS," Nature, Nature, vol. 495(7442), pages 467-473, March.
    2. Reinier Damman & Stefan Schütz & Yanzhang Luo & Markus Weingarth & Remco Sprangers & Marc Baldus, 2019. "Atomic-level insight into mRNA processing bodies by combining solid and solution-state NMR spectroscopy," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
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