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

FCP1, a phosphatase specific for the heptapeptide repeat of the largest subunit of RNA polymerase II, stimulates transcription elongation.

Molecular and cellular biology - 1 Nov 2002

Mandal Subhrangsu S, Cho Helen, Kim Sungjoon, Cabane Kettly, Reinberg Danny

Abstract excerpt

FCP1, a phosphatase specific for the carboxy-terminal domain of RNA polymerase II (RNAP II), was found to stimulate transcript elongation by RNAP II in vitro and in vivo. This activity is independent of and distinct from the elongation-stimulatory activity associated with transcription factor IIF (TFIIF), and the elongation effects of TFIIF and FCP1 were found to be additive. Genetic experiments resulted in the...

Read the complete abstract on PubMed

Topics

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

Share to Aprotinin
Share to Fungal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HeLa Cells

Share to Insecta

Share to Phosphoprotein Phosphatases

Share to Temperature

Share to Transcription Factors, TFII

Share to Transcriptional Elongation Factors

Source

Open in PubMed Open full text

Identifiers

PMID: 12370301
DOI: 10.1128/MCB.22.21.7543-7552.2002
PMCID: PMC135672

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

FCP1, a phosphatase specific for the heptapeptide repeat of the largest subunit of RNA polymerase II, stimulates transcription elongation.PMID 12370301Read ↗

A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5.Semantic proximity Read ↗

A motif shared by TFIIF and TFIIB mediates their interaction with the RNA polymerase II carboxy-terminal domain phosphatase Fcp1p in Saccharomyces cerevisiae.Semantic proximity Read ↗

Interaction of Fcp1 phosphatase with elongating RNA polymerase II holoenzyme, enzymatic mechanism of action, and genetic interaction with elongator.Semantic proximity Read ↗

An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae.Semantic proximity Read ↗

Rat1p maintains RNA polymerase II CTD phosphorylation balance.Semantic proximity Read ↗

Genetic and structural analysis of the essential fission yeast RNA polymerase II CTD phosphatase Fcp1.Semantic proximity Read ↗

RPAP1, a novel human RNA polymerase II-associated protein affinity purified with recombinant wild-type and mutated polymerase subunits.Semantic proximity Read ↗

Fip1 regulates the activity of Poly(A) polymerase through multiple interactions.Semantic proximity Read ↗

Individual letters of the RNA polymerase II CTD code govern distinct gene expression programs in fission yeast.Semantic proximity Read ↗

Defining the active site of Schizosaccharomyces pombe C-terminal domain phosphatase Fcp1.Semantic proximity Read ↗

Role for the Ssu72 C-terminal domain phosphatase in RNA polymerase II transcription elongation.Semantic proximity Read ↗

Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5.Semantic proximity Read ↗

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