Distinct cytoplasmic and nuclear fractions of Drosophila heterochromatin protein 1: their phosphorylation levels and associations with origin recognition complex proteins.

doi:10.1083/jcb.142.2.307

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Article

Distinct cytoplasmic and nuclear fractions of Drosophila heterochromatin protein 1: their phosphorylation levels and associations with origin recognition complex proteins.

The Journal of cell biology - 27 Jul 1998

Huang D W, Fanti L, Pak D T, Botchan M R, Pimpinelli S, Kellum R

Abstract excerpt

The distinct structural properties of heterochromatin accommodate a diverse group of vital chromosome functions, yet we have only rudimentary molecular details of its structure. A powerful tool in the analyses of its structure in Drosophila has been a group of mutations that reverse the repressiv...

Topics

Amino Acid Sequence
Animals
Cell Nucleus
Chromobox Protein Homolog 5
Chromosomal Proteins, Non-Histone
Cytoplasm
DNA-Binding Proteins
Drosophila
Drosophila Proteins
Heterochromatin
Insect Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Origin Recognition Complex

Phosphorylation

Protein Binding

Protein Conformation

Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 9679132
DOI: 10.1083/jcb.142.2.307
PMCID: PMC2133057

Genes

ORC2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9679132-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Distinct cytoplasmic and nuclear fractions of Drosophila heterochromatin protein 1: their phosphorylation levels and associations with origin recognition complex proteins.PMID 9679132Read ↗

Mutations in the heterochromatin protein 1 (HP1) hinge domain affect HP1 protein interactions and chromosomal distribution.Semantic proximity Read ↗

Drosophila heterochromatin protein 1 (HP1)/origin recognition complex (ORC) protein is associated with HP1 and ORC and functions in heterochromatin-induced silencing.Semantic proximity Read ↗

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

Hip, an HP1-interacting protein, is a haplo- and triplo-suppressor of position effect variegation.Semantic proximity Read ↗

HipHop interacts with HOAP and HP1 to protect Drosophila telomeres in a sequence-independent manner.Semantic proximity Read ↗

Enrichment of HP1a on Drosophila chromosome 4 genes creates an alternate chromatin structure critical for regulation in this heterochromatic domain.Semantic proximity Read ↗

Drosophila DDP1, a multi-KH-domain protein, contributes to centromeric silencing and chromosome segregation.Semantic proximity Read ↗

Heterochromatin protein 2 interacts with Nap-1 and NURF: a link between heterochromatin-induced gene silencing and the chromatin remodeling machinery in Drosophila.Semantic proximity Read ↗

The novel HP1a interactor Clump/CG30403 safeguards transposon silencing and reproductive resilience in the <i>Drosophila</i> ovarySemantic proximity Read ↗

The genomic silencing of position-effect variegation in Drosophila melanogaster: interaction between the heterochromatin-associated proteins Su(var)3-7 and HP1.Semantic proximity Read ↗

High-resolution analysis of Drosophila heterochromatin organization using SuUR Su(var)3-9 double mutants.Semantic proximity Read ↗

Heterochromatin protein 1 forms distinct complexes to direct histone deacetylation and DNA methylation.Semantic proximity Read ↗

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