High impact information on H3F3A

• Phosphorylation of histone H3 at serine 10 occurs during mitosis and meiosis in a wide range of eukaryotes and has been shown to be required for proper chromosome transmission in Tetrahymena [1].
• A chicken histone H3 gene contains intervening sequences [2].
• In contrast, lysine 4 methylation of histone H3 correlates with H3 acetylation [3].
• Chromatin immunoprecipitation of dimethylated lysine 9 on histone H3 across 53 kilobases of the chicken beta-globin locus during erythropoiesis shows an almost complete anticorrelation between regions of elevated lysine 9 methylation and acetylation [3].
• In vertebrates, centromeres lack defined sequences and are thought to be propagated by epigenetic mechanisms involving the incorporation of specialized nucleosomes containing the histone H3 variant centromere protein (CENP)-A [4].

Biological context of H3F3A

• Modulation of histone H3 variant synthesis during the myoblast-myotube transition of chicken myogenesis [5].
• Nucleotide sequences of new members (H3-IV and H3-V) of the chicken H3 histone-encoding gene family [6].
• H3-II and H3-III, respectively, possess possible AP-1- and Sp1-binding sequence elements of the forms 5'-CGAGTCAG and 5'-GGGCGGG, whereas all three H3 genes, including the previously sequenced H3-I gene, encode the same amino acid sequence [7].
• Silencing of transgene transcription precedes methylation of promoter DNA and histone H3 lysine 9 [8].
• We show that the kinetics of silencing exclude histone H3 K9 and promoter DNA methylation as the primary causative events in our transgene system [8].

Anatomical context of H3F3A

• The C-terminal hexapeptide of histone H3 of chicken erythrocytes (residues 130-135) corresponding to the sequence Ile-Arg-Gly-Glu-Arg-Ala ( IRGERA ) was prepared by solid-phase peptide synthesis and, after coupling to bovine serum albumin, was used to elicit antibodies in rabbits [9].
• Targeted disruption of an H3-IV/H3-V gene pair causes increased expression of the remaining H3 genes in the chicken DT40 cell line [10].
• In the DT40 chicken B cell line, H3-IV and H3-V, which are located in inverted orientation and share a 3'-untranslated region of 531 bp, produce about 24% of the steady-state level of total mRNAs from all the H3 genes [10].
• The reactivity of chick erythrocyte and calf thymus histone H3 thiol groups toward 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) has been investigated both in the soluble, DNA-free state and in various nucleohistone complexes [11].
• The competition between histones and low-molecular-weight chelators for Ni(II) in the cell nucleus, histidine and glutathione, is discussed on the basis of the above results, indicating that histone H3 is very likely to bind Ni(II) dissolved intracellularly from phagocytosed particulate nickel compounds [12].

Associations of H3F3A with chemical compounds

• Small amounts of chymotrypsin rapidly and selectively cleaved at leucine 20 of histone H3 [13].
• Finally, we find that although the fluorescence emission intensity of acetylethylenediamine-(1,5)-naphthol sulfonate-modified histone H3 is sensitive to octamer structure, SWI-SNF action does not alter fluorescence emission intensity [14].
• We show here that different photo-cross-links form when these particles are prepared from H3 labeled with photoaffinity reagents on the unique histone H3 cysteine [15].
• Substitution of Cys 110 of chicken histone H3 with N-iodoacetyl-N1-(5-sulpho-1-naphthyl)ethylenediamine or iodoacetamide prevents octamer formation in 2 M NaCl but does not prevent polyglutamic acid-mediated core particle assembly [16].
• The intrinsic fluorescence of tryptophan is quenched by the labelled histone H3, but not by iodide, suggesting that non-histone (tryptophan-containing) proteins lie in close proximity to the labelled histone H3 but are not immediately accessible to external solvent [17].

Other interactions of H3F3A

• In undifferentiated monoblasts, the lysozyme regulatory regions are marked by the presence of monomethylated histone H3 lysine 4, which becomes increasingly converted into trimethylated H3 lysine K4 during cell differentiation [18].
• In addition, histone hyperacetylation and dimethylation of histone H3 K4 are not uniform features of the nuclease-sensitive mouse beta-globin domain but rather define distinct subdomains within it [19].
• To directly test for a role in proliferation, explants were immunostained with antibodies against phospho-histone H3 [20].
• Binding of non-histone chromosomal protein HMG1 to histone H3 in nucleosomes detected by photochemical cross-linking [21].
• Chromatin immunoprecipitation assays showed that the ovalbumin control region was associated with acetylated histone H3 but not with dimethylated histone H3 at Lys 27 [22].

Analytical, diagnostic and therapeutic context of H3F3A

• Three of the isolated lambda recombinants have been analyzed by restriction enzyme mapping and Southern blotting; one histone H3 gene-encoding recombinant was further analyzed by DNA sequence determination [23].
• Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers [24].
• Peptide mapping of the novel H3-H4 and H3-H2B dimers showed that Cys-110 of histone H3 is cross-linked to the 18 amino acid C-terminal end of H4 or to the 66 amino acid C-terminal half of H2B [15].
• In addition, protein sequence comparison of several vertebrate species revealed that the RT-PCR strategy we have developed for isolating the chicken centromeric histone H3 variant gene should be applicable to the isolation of CENP-A from a wide range of vertebrates [25].

References