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DNA-dependent phase separation by human SSB2 (NABP1/OBFC2A) protein points to adaptations to eukaryotic genome repair processes.
Kovács, Zoltán J; Harami, Gábor M; Pálinkás, János; Kuljanishvili, Natalie; Hegedüs, József; Harami-Papp, Hajnalka; Mahmudova, Lamiya; Khamisi, Lana; Szakács, Gergely; Kovács, Mihály.
Afiliación
  • Kovács ZJ; ELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
  • Harami GM; HUN-REN-ELTE Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
  • Pálinkás J; ELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
  • Kuljanishvili N; ELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
  • Hegedüs J; ELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
  • Harami-Papp H; ELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
  • Mahmudova L; ELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
  • Khamisi L; ELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
  • Szakács G; ELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
  • Kovács M; HUN-REN Institute of Molecular Life Sciences, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
Protein Sci ; 33(4): e4959, 2024 Apr.
Article en En | MEDLINE | ID: mdl-38511671
ABSTRACT
Single-stranded DNA binding proteins (SSBs) are ubiquitous across all domains of life and play essential roles via stabilizing and protecting single-stranded (ss) DNA as well as organizing multiprotein complexes during DNA replication, recombination, and repair. Two mammalian SSB paralogs (hSSB1 and hSSB2 in humans) were recently identified and shown to be involved in various genome maintenance processes. Following our recent discovery of the liquid-liquid phase separation (LLPS) propensity of Escherichia coli (Ec) SSB, here we show that hSSB2 also forms LLPS condensates under physiologically relevant ionic conditions. Similar to that seen for EcSSB, we demonstrate the essential contribution of hSSB2's C-terminal intrinsically disordered region (IDR) to condensate formation, and the selective enrichment of various genome metabolic proteins in hSSB2 condensates. However, in contrast to EcSSB-driven LLPS that is inhibited by ssDNA binding, hSSB2 phase separation requires single-stranded nucleic acid binding, and is especially facilitated by ssDNA. Our results reveal an evolutionarily conserved role for SSB-mediated LLPS in the spatiotemporal organization of genome maintenance complexes. At the same time, differential LLPS features of EcSSB and hSSB2 point to functional adaptations to prokaryotic versus eukaryotic genome metabolic contexts.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ADN / Separación de Fases Límite: Animals / Humans Idioma: En Revista: Protein Sci Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Estados Unidos
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ADN / Separación de Fases Límite: Animals / Humans Idioma: En Revista: Protein Sci Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Estados Unidos