BAIT

ESS1

PIN1, PTF1, peptidylprolyl isomerase ESS1, L000000587, YJR017C
Peptidylprolyl-cis/trans-isomerase (PPIase); specific for phosphorylated serine and threonine residues N-terminal to proline; regulates phosphorylation of the RNAP II large subunit (Rpo21p) C-terminal domain (CTD); associates with phospho-Ser5 form of RNAP II in vivo; regulates phosphorylation of Ser7 within CTD; present along entire coding length of genes; represses initiation of CUTs; required for efficient termination of mRNA transcription and trimethylation of histone H3
Saccharomyces cerevisiae (S288c)

Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Publication

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

Wu X, Wilcox CB, Devasahayam G, Hackett RL, Arevalo-Rodriguez M, Cardenas ME, Heitman J, Hanes SD

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 ... [more]

EMBO J. Jul. 17, 2000; 19(14);3727-38 [Pubmed: 10899126]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Curated By

  • BioGRID