Matches in SemOpenAlex for { <https://semopenalex.org/work/W4308173679> ?p ?o ?g. }
- W4308173679 abstract "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 proteins. These proteins are characterized by domains rich in arginine and serine (RS domains), which are essential to alternative splicing, in vivo phase separation, and 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 spanning the human proteome indicates that RRM domains involved in phase separation have more exposed aromatic residues and that in phase-separating proteins containing RS repeats, such residues are frequently surrounded by acidic residues. 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.
- W4308173679 created "2022-11-08" @default.
- W4308173679 creator A5043134433 @default.
- W4308173679 creator A5054030264 @default.
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- W4308173679 creator A5085915915 @default.
- W4308173679 date "2022-10-24" @default.
- W4308173679 modified "2023-09-27" @default.
- W4308173679 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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- W4308173679 doi "https://doi.org/10.1101/2022.10.24.511151" @default.
- W4308173679 hasPublicationYear "2022" @default.
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