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Gene Review

FPR4  -  peptidylprolyl isomerase FPR4

Saccharomyces cerevisiae S288c

Synonyms: FK506-binding protein 4, L9324.3, PPIase, Peptidyl-prolyl cis-trans isomerase, Rotamase, ...
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Disease relevance of FPR4

  • In the yeast Saccharomyces cerevisiae, an unusual complex of Hsp70 and J-type chaperones associates with ribosome-bound nascent chains, whereas in Escherichia coli the ribosome-associated peptidyl-prolyl-cis-trans isomerase, trigger factor, plays a predominant role [1].

High impact information on FPR4

  • These results suggest that the conformational state of P38, controlled by Fpr4, is important for methylation of H3K36 by Set2 [2].
  • The Ess1/Pin1 peptidyl-prolyl isomerase (PPIase) is thought to control mitosis by binding to cell cycle regulatory proteins and altering their activity [3].
  • These PPIases consist of an NH(2)-terminal WW domain that binds to specific phosphoserine- or phosphothreonine-proline motifs present in a subset of phosphoproteins and a COOH-terminal PPIase domain that specifically isomerizes the phosphorylated serine/threonine-proline peptide bonds [4].
  • Thus, partial unfolding of the active site of the parvulins was thought to be the cause of the deterioration of PPIase activity [5].
  • Genes encoding the peptidyl proline isomerases Fpr3p and Fpr4p, when present on multicopy plasmids, will suppress this temperature-sensitive growth phenotype [6].

Biological context of FPR4

  • Consistent with such an antagonistic role, abrogation of Fpr4 catalytic activity in vivo results in increased levels of H3K36 methylation and delayed transcriptional induction kinetics of specific genes in yeast [2].

Associations of FPR4 with chemical compounds

  • Interestingly, the peptidyl proline isomerase domains of Fpr3p and Fpr4p are not required for suppression; rather the essential sequences include about 170 highly conserved residues at the proteins' N-termini [6].


  1. Ribosome-tethered molecular chaperones: the first line of defense against protein misfolding? Craig, E.A., Eisenman, H.C., Hundley, H.A. Curr. Opin. Microbiol. (2003) [Pubmed]
  2. Proline isomerization of histone h3 regulates lysine methylation and gene expression. Nelson, C.J., Santos-Rosa, H., Kouzarides, T. Cell (2006) [Pubmed]
  3. The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery. Wu, X., Wilcox, C.B., Devasahayam, G., Hackett, R.L., Arévalo-Rodríguez, M., Cardenas, M.E., Heitman, J., Hanes, S.D. EMBO J. (2000) [Pubmed]
  4. Functional conservation of phosphorylation-specific prolyl isomerases in plants. Yao, J.L., Kops, O., Lu, P.J., Lu, K.P. J. Biol. Chem. (2001) [Pubmed]
  5. Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone. Hennig, L., Christner, C., Kipping, M., Schelbert, B., Rücknagel, K.P., Grabley, S., Küllertz, G., Fischer, G. Biochemistry (1998) [Pubmed]
  6. The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Davey, M., Hannam, C., Wong, C., Brandl, C.J. Mol. Gen. Genet. (2000) [Pubmed]
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