| 2005 |
H1X (H1x) localizes to the nucleus and is partially associated with nucleosomes; it is predominantly found in chromatin regions resistant to micrococcal nuclease digestion, resembling the distribution of the replacement histone H1.0. Its gene is solitarily located and produces polyadenylated mRNA, but unlike H1.0, its expression is not induced by growth arrest or differentiation. |
Cell fractionation, micrococcal nuclease digestion, mRNA analysis (biochemical characterization) |
Biological chemistry |
Medium |
16006241
|
| 2007 |
H1X undergoes a cell-cycle-dependent change in nuclear distribution: it accumulates in the nucleolus (specifically in condensed nucleolar chromatin) during G1 phase and is evenly distributed throughout the nucleus during S and G2 phases. The amount of H1X protein remains nearly unchanged during S phase, in contrast to replication-dependent H1 subtypes. |
Immunocytochemistry, cell synchronization, cell-cycle staging |
Biology of the cell |
Medium |
17868027
|
| 2010 |
During retinoic acid-induced differentiation of NT2 embryonal carcinoma cells, H1X is preferentially incorporated into the regulatory region of the Nanog gene (a stemness marker that is repressed upon differentiation), suggesting a repressive role for H1X at this locus. |
Chromatin immunoprecipitation (ChIP) coupled with real-time PCR, Western blot |
FEBS letters |
Medium |
20974140
|
| 2015 |
ChIP-sequencing and cell fractionation in human breast cancer cells revealed that H1X is associated with coding regions, RNA polymerase II-enriched regions, and hypomethylated CpG islands; it accumulates within constitutive or included exons and retained introns and toward the 3' end of expressed genes. H1X knockdown dysregulates a subset of genes related to cell movement and transport; up-regulated genes in H1X-depleted cells have lower-than-average H1 content and do not form an H1 valley upon induction. |
ChIP-sequencing, cell fractionation, inducible knockdown, gene expression analysis |
The Journal of biological chemistry |
High |
25645921
|
| 2019 |
NMR backbone resonance assignments of the H1X N-terminal domain and globular domain show that the N-terminal domain adopts transient alpha-helical secondary structural elements at high ionic strength (in the presence of sodium perchlorate), suggesting the N-terminal domain can assume structured conformations in conditions mimicking the presence of DNA. |
Solution NMR (backbone resonance assignment, chemical shift analysis) |
Biomolecular NMR assignments |
Medium |
30868366
|
| 2022 |
The histone chaperone TAF-Iβ recognizes H1.10 (H1X) in a 2:2 complex; the TAF-Iβ core interacts mainly through electrostatic interactions with the globular domain of H1.10. Structure-guided mutagenesis confirmed these interactions. The structural model shows that TAF-Iβ occludes the DNA-binding sites of H1.10, providing the mechanism by which TAF-Iβ functions as a chaperone by preventing H1.10 from directly binding DNA. |
Methyl-TROSY NMR with spin labels, biochemical binding assays, mutagenesis, structural modeling, comparison with chromatosome structure |
Journal of molecular biology |
High |
35870650
|
| 2024 |
ChIP-Seq profiling in a breast cancer cell line shows H1X preferentially localizes in high-GC regions (A compartment) and is enriched at recently incorporated transposable elements (SVA and SINE-Alu families). H1X depletion leads to derepression of these transposable elements, demonstrating a direct role for H1X in maintaining TE repression. |
ChIP-Seq, H1X knockdown/depletion, transposable element expression analysis |
Nucleic acids research |
High |
38261975
|
| 2024 |
Super-resolution imaging and imaging analysis in multiple human cell lines show that H1X is distributed throughout the nucleus and is universally enriched in high-GC regions and in nucleoli. H1X (but not other H1 variants) shows a distinct response to inhibition of ribosomal DNA transcription, linking its nucleolar enrichment to active rDNA transcription. H1 variant depletion affects chromatin structure in a variant-specific manner. |
Super-resolution microscopy, immunofluorescence, rDNA transcription inhibition, multiple cell lines |
eLife |
Medium |
38530350
|
| 2024 |
MEF2D transcription factor directly binds the H1X promoter and drives transcriptional activation of H1X in gastric cancer cells. H1X upregulation in turn promotes in vivo metastasis of gastric cancer cells and upregulates β-CATENIN. The IL-13/IL13RA1 signaling axis induces MEF2D and H1X expression in a time-dependent manner. |
Chromatin immunoprecipitation (ChIP), promoter-binding assay, overexpression/knockdown, proteomics, mouse metastasis models, quantitative RT-PCR |
Cancer letters |
Medium |
38609001
|
| 2024 |
Overexpression of H1X in the mouse ventral hippocampus via viral vector does not produce behavioral changes (social, anxiety-like, or memory tests) in susceptible, resilient, or unstressed mice, indicating that elevated H1X alone is not sufficient to drive behavioral adaptations to chronic social stress. |
Viral vector overexpression in vivo, chronic social defeat stress paradigm, behavioral testing |
Translational psychiatry |
Medium |
38834575
|