Heddy Soufari

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Peptidylprolyl isomerases have been implicated in chromatin regulation through their association with histones, chromatin-modifying enzymes and DNA-binding transcription factors. As with other post-translational modifications to proteins, a mechanistic understanding of the regulation of biological processes is fostered by loss-of-function studies both in(More)
Precise regulation of mRNA processing, translation, localization, and stability relies on specific interactions with RNA-binding proteins whose biological function and target preference are dictated by their preferred RNA motifs. The RBPMS family of RNA-binding proteins is defined by a conserved RNA recognition motif (RRM) domain found in metazoan(More)
Background: The yeast histone chaperone Fpr4 harbours a peptidyl-prolyl isomerase domain of the FK506-binding protein (FKBP) family. Results: Catalytic efficiency towards three peptides from histone H3 relates to residues flanking the central proline. Conclusion: Substrate residues C-terminal to the proline dictate isomerase activity by Fpr4. Significance:(More)
The FK506-binding protein (FKBP) family of peptidyl-prolyl isomerases (PPIases) is characterized by a common catalytic domain that binds to the inhibitors FK506 and rapamycin. As one of four FKBPs within the yeast Saccharomyces cerevisiae, Fpr4 has been described as a histone chaperone, and is in addition implicated in epigenetic function in part due to its(More)
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