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- W4322757989 abstract "Phase separation plays crucial roles in both sustaining cellular function and perpetuating disease states. Despite extensive studies, our understanding of this process is hindered by low solubility of phase-separating proteins. One example of this is found in SR and SR-related proteins. These proteins are characterized by domains rich in arginine and serine (RS domains), which are essential to alternative splicing and in vivo phase separation. However, they are also responsible for a low solubility that has made these proteins difficult to study for decades. Here, we solubilize the founding member of the SR family, SRSF1, by introducing a peptide mimicking RS repeats as a co-solute. We find that this RS-mimic peptide forms interactions similar to those of the protein's RS domain. Both interact with a combination of surface-exposed aromatic residues and acidic residues on SRSF1's RNA Recognition Motifs (RRMs) through electrostatic and cation-pi interactions. Analysis of RRM domains from human SR proteins indicates that these sites are conserved across the protein family. In addition to opening an avenue to previously unavailable proteins, our work provides insight into how SR proteins phase separate and participate in nuclear speckles." @default.
- W4322757989 created "2023-03-03" @default.
- W4322757989 creator A5042504962 @default.
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- W4322757989 date "2023-03-02" @default.
- W4322757989 modified "2023-09-25" @default.
- W4322757989 title "Peptides that Mimic RS repeats modulate phase separation of SRSF1, revealing a reliance on combined stacking and electrostatic interactions" @default.
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- W4322757989 doi "https://doi.org/10.7554/elife.84412" @default.
- W4322757989 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36862748" @default.
- W4322757989 hasPublicationYear "2023" @default.
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