ArticleThe Journal of biological chemistry2010
The middle region of an HP1-binding protein, HP1-BP74, associates with linker DNA at the entry/exit site of nucleosomal DNA.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Function of HP1BP3 as a linker histone is regulated by linker histone chaperones, NPM1 and TAF-I.Epigenetics & chromatin · 2025Article
- Variants in Chromatin Remodeling Genes Are Involved in Patients With Chiari Malformation Type 1.Birth defects research · 2025Article
- Stochastic chromatin packing of 3D mitotic chromosomes revealed by coherent X-rays.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A critical role of telomere chromatin compaction in ALT tumor cell growth.Nucleic acids research · 2020Article
- Local enrichment of HP1alpha at telomeres alters their structure and regulation of telomere protection.Nature communications · 2018Article
- Genomic and Proteomic Resolution of Heterochromatin and Its Restriction of Alternate Fate Genes.Molecular cell · 2017Article
- The novel transcriptional factor HP1BP3 negatively regulates Hsp70 transcription in Crassostrea hongkongensis.Scientific reports · 2017Article
- Calcium ions function as a booster of chromosome condensation.Scientific reports · 2016Article
- HP1BP3, a Chromatin Retention Factor for Co-transcriptional MicroRNA Processing.Molecular cell · 2016Article
- RNase P protein subunit Rpp29 represses histone H3.3 nucleosome deposition.Molecular biology of the cell · 2016Article
- Heterochromatin Protein 1 Binding Protein 3 Expression as a Candidate Marker of Intrinsic 5-Fluorouracil Resistance.Anticancer research · 2016Article
- A role for repressive complexes and H3K9 di-methylation in PRDM5-associated brittle cornea syndrome.Human molecular genetics · 2015Article
- HP1BP3 is a novel histone H1 related protein with essential roles in viability and growth.Nucleic acids research · 2015Article
- Profiling of the Chromatin-associated Proteome Identifies HP1BP3 as a Novel Regulator of Cell Cycle Progression.Molecular & cellular proteomics : MCP · 2014Article
- Characterization of native protein complexes and protein isoform variation using size-fractionation-based quantitative proteomics.Molecular & cellular proteomics : MCP · 2013Article
- The proteomic investigation of chromatin functional domains reveals novel synergisms among distinct heterochromatin components.Molecular & cellular proteomics : MCP · 2013Article
- DNA methylation: superior or subordinate in the epigenetic hierarchy?Genes & cancer · 2011Article
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Authors and funding
14 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In higher eukaryotic cells, DNA molecules are present as chromatin fibers, complexes of DNA with various types of proteins; chromatin fibers are highly condensed in metaphase chromosomes during mitosis. Although the formation of the metaphase chromosome structure is essential for the equal segregation of replicated chromosomal DNA into the daughter cells, the mechanism involved in the organization of metaphase chromosomes is poorly understood. To identify proteins involved in the formation and/or maintenance of metaphase chromosomes, we examined proteins that dissociated from isolated human metaphase chromosomes by 0.4 m NaCl treatment; this treatment led to significant chromosome decondensation, but the structure retained the core histones. One of the proteins identified, HP1-BP74 (heterochromatin protein 1-binding protein 74), composed of 553 amino acid residues, was further characterized. HP1-BP74 middle region (BP74Md), composed of 178 amino acid residues (Lys(97)-Lys(274)), formed a chromatosome-like structure with reconstituted mononucleosomes and protected the linker DNA from micrococcal nuclease digestion by approximately 25 bp. The solution structure determined by NMR revealed that the globular domain (Met(153)-Thr(237)) located within BP74Md possesses a structure similar to that of the globular domain of linker histones, which underlies its nucleosome binding properties. Moreover, we confirmed that BP74Md and full-length HP1-BP74 directly binds to HP1 (heterochromatin protein 1) and identified the exact sites responsible for this interaction. Thus, we discovered that HP1-BP74 directly binds to HP1, and its middle region associates with linker DNA at the entry/exit site of nucleosomal DNA in vitro.
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