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Mol Genet Genomics 2014 Apr 3;289(2):125-36. Epub 2013 Dec 3.

Department of Pediatrics, Children's Research Institute, Human and Molecular Genetics Center, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI, USA,

Fpr3 and Fpr4 of Saccharomyces cerevisiae are nuclear FK506-binding proteins each containing an extended acidic domain in addition to the conserved FK506-binding/peptidylprolyl isomerase (PPIase) domain. Previous studies have shown that the PPIase domain regulates histone H3 methylation, while the acidic domain facilitates histone deposition and may regulate rDNA silencing. To gain insight into the role of FKBPs in maintaining chromatin structure, we examined the transcriptional profiles of fpr3 (-) and fpr4 (-) cells. Read More

Cell 2006 Sep;126(5):905-16

Gurdon Institute and Department of Pathology, Tennis Court Road, Cambridge, CB2 1QR, UK.

The cis-trans isomerization of proline serves as a regulatory switch in signaling pathways. We identify the proline isomerase Fpr4, a member of the FK506 binding protein family in Saccharomyces cerevisiae, as an enzyme which binds the amino-terminal tail of histones H3 and H4 and catalyses the isomerization of H3 proline P30 and P38 in vitro. We show that P38 is necessary for methylation of K36 and that isomerization by Fpr4 inhibits the ability of Set2 to methylate H3 K36 in vitro. Read More