High impact information on Hist1h1c

• Involvement of histone H1.2 in apoptosis induced by DNA double-strand breaks [1].
• These results indicate that histone H1.2 plays an important role in transmitting apoptotic signals from the nucleus to the mitochondria following DNA double-strand breaks [1].
• H1.2-deficient mice exhibited increased cellular resistance in thymocytes and the small intestine to X-ray-induced apoptosis [1].
• Histone H1.2 has only one tyrosine residue in the entire molecule, which ensures the exact position of the substrate to be involved [2].
• To further investigate the in vivo role of individual mammalian H1s in development, we generated mice lacking H1c, H1d, or H1e by homologous recombination in mouse embryonic stem cells [3].

Biological context of Hist1h1c

• The phosphorylation preferentially occurred in a single H1 subtype (H1c) among the five (H1a-e) fractionated by high performance liquid chromatography [4].
• In a "physiological" range of H1:DNA ratios only H1e, at variance from H1c, was found to cause a marked inhibition of in vitro enzymic DNA methylation [5].
• Overexpression of H1c to comparable levels had no effect on cell cycle progression [6].

Anatomical context of Hist1h1c

• Transcription of the subtype genes H1.2 and H1.4 was found in all tissues and cell lines studied [7].
• Whole-mount in situ hybridization using cloned H1c and H1e cDNAs revealed that the mRNAs were present in the cytoplasm of oocytes and 1-cell embryos, in contrast to the sea urchin early embryo where they are sequestered in the cell nucleus [8].
• Radiolabeling revealed that species comigrating with the somatic H1 subtypes H1a and H1c were synthesized in maturing oocytes and in one- and two-cell embryos [9].
• The principal histone H1 subtypes of mouse prepachytene spermatocytes were identified as H1a and H1c, proteins that are metabolically unstable and have been postulated to promote extended or flexible chromatin conformations [10].
• Under these experimental conditions the histone H1 variants H1b and H1c obtained from mitotic enriched NIH 3T3 fibroblasts and isolated by reversed-phase high-performance liquid chromatography were clearly separated in their non-phosphorylated and different phosphorylated forms [11].

Associations of Hist1h1c with chemical compounds

• A triethylammonium methanephosphonate system proved efficacious for the separation of rat histone subtype H1c from H1e and a perchlorate/triethylammonium phosphate system for the analysis of chicken and mouse linker histones [12].

Other interactions of Hist1h1c

• To determine whether one of these H1s, in particular, was responsible for the compensation present in H1(0-/-) mice, each of the three H1 knockout mouse lines was bred with H1(0) knockout mice to generate H1c/H1(0), H1d/H1(0), or H1e/H1(0) double-knockout mice [3].
• The results indicate that 1) the response of H1 subtypes to cAMP-dependent protein kinase in vivo and in vitro is H1 subtype-specific, and 2) the H1c phosphorylation may play an important role in the restrictive area of chromatin in both cell differentiation and hormonal stimulation mediated by cAMP [4].
• Therefore, in these cells, H1t seems not to be replaced by H1.1 or H1.2 [13].
• We were also able to induce major alterations in the normal stoichiometry of chromatin-associated H1 variants through overproduction of H1c and H1e [14].

Analytical, diagnostic and therapeutic context of Hist1h1c

• H1e and H1c histone variants were purified from mouse L929 fibroblasts using a reverse phase HPLC, and their effect on in vitro DNA methylation was investigated, together with their ability to bind unmethylated or methylated CpG-rich 44bp oligonucleotides [5].

References