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The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery.

The Ess1/Pin1 peptidyl-prolyl isomerase (PPIase) is thought to control mitosis by binding to cell cycle regulatory proteins and altering their activity. Here we isolate temperature-sensitive ess1 mutants and identify six multicopy suppressors that rescue their mitotic-lethal phenotype. None are cell cycle regulators. Instead, five encode proteins involved in transcription that bind DNA, modify chromatin structure or are regulatory subunits of RNA polymerase II. A sixth suppressor, cyclophilin A, is a member of a distinct family of PPIases that are targets of immuno suppressive drugs. We show that the expression of some but not all genes is decreased in ess1 mutants, and that Ess1 interacts with the C-terminal domain (CTD) of RNA polymerase II in vitro and in vivo. The results forge a strong link between PPIases and the transcription machinery and suggest a new model for how Ess1/Pin1 controls mitosis. In this model, Ess1 binds and isomerizes the CTD of RNA polymerase II, thus altering its interaction with proteins required for transcription of essential cell cycle genes.

Pubmed ID: 10899126


  • Wu X
  • Wilcox CB
  • Devasahayam G
  • Hackett RL
  • Arévalo-Rodríguez M
  • Cardenas ME
  • Heitman J
  • Hanes SD


The EMBO journal

Publication Data

July 17, 2000

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Chromatin
  • Drosophila
  • Fungal Proteins
  • Gene Expression Regulation, Fungal
  • Humans
  • Immunophilins
  • Mediator Complex
  • Mitosis
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Peptidylprolyl Isomerase
  • Phenotype
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA Polymerase II
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sequence Alignment
  • Structure-Activity Relationship
  • Suppression, Genetic
  • Tacrolimus Binding Proteins
  • Transcription Factors
  • Transcription, Genetic