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  1. Artikel ; Online: Heterotypic interactions can drive selective co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex.

    Davis, Richoo B / Supakar, Anushka / Ranganath, Aishwarya Kanchi / Moosa, Mahdi Muhammad / Banerjee, Priya R

    Nature communications

    2024  Band 15, Heft 1, Seite(n) 1168

    Abstract: Prion-like domains (PLDs) are low-complexity protein sequences enriched within nucleic acid-binding proteins including those involved in transcription and RNA processing. PLDs of FUS and EWSR1 play key roles in recruiting chromatin remodeler mammalian ... ...

    Abstract Prion-like domains (PLDs) are low-complexity protein sequences enriched within nucleic acid-binding proteins including those involved in transcription and RNA processing. PLDs of FUS and EWSR1 play key roles in recruiting chromatin remodeler mammalian SWI/SNF (mSWI/SNF) complex to oncogenic FET fusion protein condensates. Here, we show that disordered low-complexity domains of multiple SWI/SNF subunits are prion-like with a strong propensity to undergo intracellular phase separation. These PLDs engage in sequence-specific heterotypic interactions with the PLD of FUS in the dilute phase at sub-saturation conditions, leading to the formation of PLD co-condensates. In the dense phase, homotypic and heterotypic PLD interactions are highly cooperative, resulting in the co-mixing of individual PLD phases and forming spatially homogeneous condensates. Heterotypic PLD-mediated positive cooperativity in protein-protein interaction networks is likely to play key roles in the co-phase separation of mSWI/SNF complex with transcription factors containing homologous low-complexity domains.
    Mesh-Begriff(e) Animals ; Prions/metabolism ; Transcription Factors/metabolism ; Chromatin ; Mammals/genetics ; Chromatin Assembly and Disassembly
    Chemische Substanzen Prions ; Transcription Factors ; Chromatin
    Sprache Englisch
    Erscheinungsdatum 2024-02-07
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-44945-5
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Heterotypic interactions in the dilute phase can drive co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex.

    Davis, Richoo B / Supakar, Anushka / Ranganath, Aishwarya Kanchi / Moosa, Mahdi Muhammad / Banerjee, Priya R

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Prion-like domains (PLDs) are low-complexity protein sequences enriched within nucleic acid-binding proteins including those involved in transcription and RNA processing. PLDs of FUS and EWSR1 play key roles in recruiting chromatin remodeler mammalian ... ...

    Abstract Prion-like domains (PLDs) are low-complexity protein sequences enriched within nucleic acid-binding proteins including those involved in transcription and RNA processing. PLDs of FUS and EWSR1 play key roles in recruiting chromatin remodeler mammalian SWI/SNF complex to oncogenic FET fusion protein condensates. Here, we show that disordered low-complexity domains of multiple SWI/SNF subunits are prion-like with a strong propensity to undergo intracellular phase separation. These PLDs engage in sequence-specific heterotypic interactions with the PLD of FUS in the dilute phase at sub-saturation conditions, leading to the formation of PLD co-condensates. In the dense phase, homotypic and heterotypic PLD interactions are highly cooperative, resulting in the co-mixing of individual PLD phases and forming spatially homogeneous co-condensates. Heterotypic PLD-mediated positive cooperativity in protein-protein interaction networks is likely to play key roles in the co-phase separation of mSWI/SNF complex with transcription factors containing homologous low-complexity domains.
    Sprache Englisch
    Erscheinungsdatum 2023-11-22
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.04.12.536623
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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