Cargando…
Arg/Lys-containing IDRs are cryptic binding domains for ATP and nucleic acids that interplay to modulate LLPS
Most membrane-less organelles (MLOs) formed by LLPS contain both nucleic acids and IDR-rich proteins. Currently while IDRs are well-recognized to drive LLPS, nucleic acids are thought to exert non-specific electrostatic/salt effects. TDP-43 functions by binding RNA/ssDNA and its LLPS was characteriz...
Autores principales: | Dang, Mei, Li, Tongyang, Zhou, Shibo, Song, Jianxing |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9712531/ https://www.ncbi.nlm.nih.gov/pubmed/36450893 http://dx.doi.org/10.1038/s42003-022-04293-w |
Ejemplares similares
-
ATP and nucleic acids competitively modulate LLPS of the SARS-CoV2 nucleocapsid protein
por: Dang, Mei, et al.
Publicado: (2023) -
CTD of SARS‐CoV‐2 N protein is a cryptic domain for binding ATP and nucleic acid that interplay in modulating phase separation
por: Dang, Mei, et al.
Publicado: (2021) -
ATP biphasically modulates LLPS of SARS-CoV-2 nucleocapsid protein and specifically binds its RNA-binding domain
por: Dang, Mei, et al.
Publicado: (2021) -
ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues
por: Dang, Mei, et al.
Publicado: (2021) -
Structural basis of anti-SARS-CoV-2 activity of HCQ: specific binding to N protein to disrupt its interaction with nucleic acids and LLPS
por: Dang, Mei, et al.
Publicado: (2021)