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Article

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

Biochemistry - 26 Apr 2005

Li Zhong, Li Hongmin, Devasahayam Gina, Gemmill Trent, Chaturvedi Vishnu, Hanes Steven D, Van Roey Patrick

Abstract excerpt

Ess1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that binds to the carboxy-terminal domain (CTD) of RNA polymerase II. Ess1 is thought to function by inducing conformational changes in the CTD that control the assembly of cofactor complexes on the transcription unit. Ess1 (also called Pin1) is highly conserved throughout the eukaryotic kingdom and is required for growth in some species, including the human...

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Identifiers

PMID: 15835905
DOI: 10.1021/bi050115l
PMCID: PMC4773908

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

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Click a neighbor to travelStep 1 · 12 closest

The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility.PMID 15835905Read ↗

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

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

Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae.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 dispensable for growth but required for virulence in Cryptococcus neoformans.Semantic proximity Read ↗

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

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

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 ↗

Activity and Affinity of Pin1 Variants.Semantic proximity Read ↗

The kingdom of the prolyl-isomerase Pin1: The structural and functional convergence and divergence of Pin1Semantic proximity Read ↗

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

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