Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Current genetics - 1 Dec 2001

Wu X, Chang A, Sudol M, Hanes S D

Abstract excerpt

Transcription of protein-coding genes by RNA polymerase II (pol II) is a highly coordinated process that requires the stepwise association of distinct protein complexes with the C-terminal domain (CTD) of Rpbl, the largest subunit of RNA pol II. Interaction of these complexes with the CTD might be subject to regulation by proteins such as Ess1 and Rsp5. Ess1, a prolyl-isomerase, binds the CTD and is thought to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding, Competitive
Share to Cyclin-Dependent Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endosomal Sorting Complexes Required for Transport

Share to NIMA-Interacting Peptidylprolyl Isomerase

Share to Peptidylprolyl Isomerase

Share to Phosphoprotein Phosphatases

Share to RNA Polymerase II

Share to Ubiquitin-Protein Ligase Complexes

Source

Identifiers

PMID: 11795843
DOI: 10.1007/s00294-001-0257-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Genetic interactions between the ESS1 prolyl-isomerase and the RSP5 ubiquitin ligase reveal opposing effects on RNA polymerase II function.PMID 11795843Read ↗

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

Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae.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 is required for transcription termination of small noncoding RNAs via the Nrd1 pathway.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 structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility.Semantic proximity Read ↗

The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme.Semantic proximity Read ↗

Functional domains of the Rsp5 ubiquitin-protein ligase.Semantic proximity Read ↗

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

Rsc4 connects the chromatin remodeler RSC to RNA polymerases.Semantic proximity Read ↗

Role of RNA polymerase II carboxy terminal domain phosphorylation in DNA damage response.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.