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

Regulation of transcription by H1 phosphorylation in Tetrahymena is position independent and requires clustered sites.

Proceedings of the National Academy of Sciences of the United States of America - 30 Apr 2002

Dou Yali, Gorovsky Martin A

Abstract excerpt

In Tetrahymena cells, constitutive phosphorylation of histone H1 phenocopies the loss of H1 from chromatin. Regulation of transcription by H1 phosphorylation is achieved by altering the overall charges of a small domain. Here, we further explore the electrostatic properties of this domain and the...

Read the complete abstract on PubMed

Topics

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

Share to Blotting, Northern
Share to Cell Nucleus
Share to Electrophysiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histones

Share to Phosphorylation

Share to Protein Structure, Tertiary

Share to Tetrahymena

Share to Transcription, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 11972045
DOI: 10.1073/pnas.092029599
PMCID: PMC122916

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-11972045-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulation of transcription by H1 phosphorylation in Tetrahymena is position independent and requires clustered sites.PMID 11972045Read ↗

Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin.Semantic proximity Read ↗

Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal.Semantic proximity Read ↗

The role of electrostatic interactions in the phase separation of HP1α and its protein binding partnersSemantic proximity Read ↗

Single-Molecule Studies of the Linker Histone H1 Binding to DNA and the Nucleosome.Semantic proximity Read ↗

Interplay between charge distribution and DNA in shaping HP1 paralog phase separation and localizationSemantic proximity Read ↗

Phosphorylation of heterochromatin protein 1 by casein kinase II is required for efficient heterochromatin binding in Drosophila.Semantic proximity Read ↗

Nuclear partitioning by surface condensation on metaphase chromatidsSemantic proximity Read ↗

The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo.Semantic proximity Read ↗

N-terminal phosphorylation of HP1{alpha} promotes its chromatin binding.Semantic proximity Read ↗

Mitotic phosphorylation prevents the binding of HMGN proteins to chromatin.Semantic proximity Read ↗

Probing the hierarchical dynamics of DNA-sperm nuclear transition protein complex through fuzzy interaction and mesoscale condensationSemantic proximity Read ↗

Transcription-induced active forces suppress chromatin motionSemantic proximity Read ↗

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