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Single-stranded nucleic acid binding and coacervation by linker histone H1.
Leicher, Rachel; Osunsade, Adewola; Chua, Gabriella N L; Faulkner, Sarah C; Latham, Andrew P; Watters, John W; Nguyen, Tuan; Beckwitt, Emily C; Christodoulou-Rubalcava, Sophia; Young, Paul G; Zhang, Bin; David, Yael; Liu, Shixin.
Afiliación
  • Leicher R; Laboratory of Nanoscale Biophysics and Biochemistry, The Rockefeller University, New York, NY, USA.
  • Osunsade A; Tri-Institutional PhD Program in Chemical Biology, New York, NY, USA.
  • Chua GNL; Tri-Institutional PhD Program in Chemical Biology, New York, NY, USA.
  • Faulkner SC; Chemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center (MSKCC), New York, NY, USA.
  • Latham AP; Laboratory of Nanoscale Biophysics and Biochemistry, The Rockefeller University, New York, NY, USA.
  • Watters JW; Tri-Institutional PhD Program in Chemical Biology, New York, NY, USA.
  • Nguyen T; Chemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center (MSKCC), New York, NY, USA.
  • Beckwitt EC; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
  • Christodoulou-Rubalcava S; Laboratory of Nanoscale Biophysics and Biochemistry, The Rockefeller University, New York, NY, USA.
  • Young PG; Laboratory of Nanoscale Biophysics and Biochemistry, The Rockefeller University, New York, NY, USA.
  • Zhang B; Tri-Institutional MD-PhD Program, New York, NY, USA.
  • David Y; Laboratory of DNA Replication, Howard Hughes Medical Institute, The Rockefeller University, New York, NY, USA.
  • Liu S; Tri-Institutional PhD Program in Chemical Biology, New York, NY, USA.
Nat Struct Mol Biol ; 29(5): 463-471, 2022 05.
Article en En | MEDLINE | ID: mdl-35484234
The H1 linker histone family is the most abundant group of eukaryotic chromatin-binding proteins. However, their contribution to chromosome structure and function remains incompletely understood. Here we use single-molecule fluorescence and force microscopy to directly visualize the behavior of H1 on various nucleic acid and nucleosome substrates. We observe that H1 coalesces around single-stranded DNA generated from tension-induced DNA duplex melting. Using a droplet fusion assay controlled by optical tweezers, we find that single-stranded nucleic acids mediate the formation of gel-like H1 droplets, whereas H1-double-stranded DNA and H1-nucleosome droplets are more liquid-like. Molecular dynamics simulations reveal that multivalent and transient engagement of H1 with unpaired DNA strands drives their enhanced phase separation. Using eGFP-tagged H1, we demonstrate that inducing single-stranded DNA accumulation in cells causes an increase in H1 puncta that are able to fuse. We further show that H1 and Replication Protein A occupy separate nuclear regions, but that H1 colocalizes with the replication factor Proliferating Cell Nuclear Antigen, particularly after DNA damage. Overall, our results provide a refined perspective on the diverse roles of H1 in genome organization and maintenance, and indicate its involvement at stalled replication forks.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Histonas / Nucleosomas Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Histonas / Nucleosomas Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos