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Article

A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus.

The Journal of cell biology - 1 Nov 1994

Benton B M, Zang J H, Thorner J

Abstract excerpt

The gene (FPR3) encoding a novel type of peptidylpropyl-cis-trans-isomerase (PPIase) was isolated during a search for previously unidentified nuclear proteins in Saccharomyces cerevisiae. PPIases are thought to act in conjunction with protein chaperones because they accelerate the rate of conformational interconversions around proline residues in polypeptides. The FPR3 gene product (Fpr3) is 413 amino acids long....

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Source

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Identifiers

PMID: 7525596
DOI: 10.1083/jcb.127.3.623
PMCID: PMC2120238

Genes

FPR3
FPR1
FPR2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus.PMID 7525596Read ↗

Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast.Semantic proximity Read ↗

Saccharomyces cerevisiae Fpr1 functions as a chaperone to inhibit protein aggregation.Semantic proximity Read ↗

Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity.Semantic proximity Read ↗

Immunosuppressant target protein FKBP12 is required for P-glycoprotein function in yeast.Semantic proximity Read ↗

Fpr1, a primary target of rapamycin, functions as a transcription factor for ribosomal protein genes cooperatively with Hmo1 in Saccharomyces cerevisiaeSemantic proximity Read ↗

Loss-of-function pdr3 mutations convert the Pdr3p transcription activator to a protein suppressing multidrug resistance in Saccharomyces cerevisiae.Semantic proximity Read ↗

Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase.Semantic proximity Read ↗

Antifungal properties of the immunosuppressant FK-506: identification of an FK-506-responsive yeast gene distinct from FKB1.Semantic proximity Read ↗

FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisiae.Semantic proximity Read ↗

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Rapamycin Antifungal Action Is Mediated via Conserved Complexes with FKBP12 and TOR Kinase Homologs in Cryptococcus neoformansSemantic proximity Read ↗

Physiological function of FKBP12, a primary target of rapamycin/FK506: a newly identified role in transcription of ribosomal protein genes in yeastSemantic proximity Read ↗

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