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Article

Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae.

The Journal of biological chemistry - 22 Apr 2005

Gemmill Trent R, Wu Xiaoyun, Hanes Steven D

Abstract excerpt

Ess1 is an essential peptidylprolyl-cis/trans-isomerase in the yeast Saccharomyces cerevisiae. Ess1 and its human homolog, Pin1, bind to phospho-Ser-Pro sites within proteins, including the carboxyl-terminal domain (CTD) of Rpb1, the largest subunit of RNA polymerase II (pol II). Ess1 and Pin1 are thought to control mRNA synthesis by catalyzing conformational changes in Rpb1 that affect interaction of cofactors...

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PMID: 15728580
DOI: 10.1074/jbc.M412172200

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

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Related research

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Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae.PMID 15728580Read ↗

Genetic interactions with C-terminal domain (CTD) kinases and the CTD of RNA Pol II suggest a role for ESS1 in transcription initiation and elongation in Saccharomyces cerevisiae.Semantic proximity Read ↗

The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility.Semantic proximity Read ↗

Functional interaction of the Ess1 prolyl isomerase with components of the RNA polymerase II initiation and termination machineries.Semantic proximity Read ↗

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

The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae.Semantic proximity Read ↗

The Ess1 prolyl isomerase is required for growth and morphogenetic switching in Candida albicans.Semantic proximity Read ↗

Genetic interactions between the ESS1 prolyl-isomerase and the RSP5 ubiquitin ligase reveal opposing effects on RNA polymerase II function.Semantic proximity Read ↗

Crosstalk of prolyl isomerases, Pin1/Ess1, and cyclophilin A.Semantic proximity Read ↗

The Ess1 prolyl isomerase is dispensable for growth but required for virulence in Cryptococcus neoformans.Semantic proximity Read ↗

Functionally important residues in the peptidyl-prolyl isomerase Pin1 revealed by unigenic evolution.Semantic proximity Read ↗

The Ess1 prolyl isomerase is required for transcription termination of small noncoding RNAs via the Nrd1 pathway.Semantic proximity Read ↗

Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13.Semantic proximity Read ↗

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