Disease relevance of HIST2H4A

• H2A and H4 were digested with Staphylococcus aureus V8 protease, and the digests were separated by RP-HPLC [1].
• Therefore, we designed a new histone H4 gene with codons optimized for the E. coli expression system and constructed the H4 gene by chemically synthesized oligodeoxyribonucleotides [2].

High impact information on HIST2H4A

• The human histone H4 gene FO108 is regulated during the cell cycle with a peak in transcription during early S phase [3].
• H2A and H2B histone genes were located at one end of the insert and H4 gene at the other with a 3.1 kb spacer in between [4].
• Protein-DNA interactions in the 5' promoter region of a cell cycle-regulated human H4 histone gene have been analyzed at single-nucleotide resolution in vivo [5].
• A human histone gene cluster was assigned to chromosome 1 by Southern blot analysis of DNA's from a series of mouse-human somatic cell hybrids with 32P-labeled cloned human H4 and H3 histone DNA as probes [6].
• In chronically infected cells treated with a phorbol ester, we found that acetylation of both histones H3 and H4 occurs at discrete nucleosomal regions before the onset of viral mRNA transcription [7].

Biological context of HIST2H4A

• We conclude that H4 gene transcription during differentiation is downregulated by modulating protein interaction at the site II cell cycle element and that retention of an open chromatin conformation may be associated with site I occupancy [8].
• A human H4 histone gene was isolated and the nucleotide sequences of the mRNA coding as well as the 5' and 3' flanking regions were determined [9].
• Deletion mutants were constructed by BAL-31 nuclease digestion of sequences in the 5' flanking region of this H4 histone gene and were assayed in an in vitro transcription system [9].
• A series of sequences which have been assigned putative regulatory roles in histone genes and/or in other genes were identified both upstream and downstream from the H4 histone protein coding region [9].
• In addition to the histone genes on these clusters, only two other genes containing the stem-loop sequence were identified, a histone H4 gene on human chromosome 12 (mouse chromosome 6) and the previously described H2a.X gene located on human chromosome 11 [10].

Anatomical context of HIST2H4A

• Micrococcal nuclease, DNase I, and restriction enzymes show similar cleavage sites and levels of sensitivity at the H4/n locus in both proliferating and differentiated HL-60 cells [8].
• Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes [1].
• Using a nuclease S1 assay, we detected about 10,000 transcripts encoding both late H3 and H4 proteins in the unfertilized egg [11].
• We have investigated the promoter element(s) required by the cell cycle regulated FO108 human histone H4 gene for control of gene expression during adipocyte proliferation and differentiation [12].

Associations of HIST2H4A with chemical compounds

• Acetylation of H4 was inhibited by Lys-coenzyme A (CoA), a selective inhibitor of p300 acetyltransferase activity [13].
• Models of 12 (R) HETE, 12 (S) HETE (the "S" isomer of 12 (R) HETE), and 8 (R) hydroxy-hexadecatrienoic acid [8 (R) HHDTrE, a catabolic isomer of 12 (R) HETE] were formed and docked with phosphatidyl choline and the H3-H4 peptide of the alpha-subunit of Na,K-ATPase [14].
• The hH4 cDNA was subcloned into the pQE30 expression vector, in frame with a sequence encoding an N-terminal stretch of six histidine residues [15].

Physical interactions of HIST2H4A

• BRDT specifically binds hyperacetylated histone H4 tail depending on the integrity of both bromodomains [16].

Other interactions of HIST2H4A

• The proliferation-specific transcription factor complex HiNF-D interacts with sequence specificity in a proximal promoter element of the human H4 histone gene FO108, designated Site II [17].
• Performance of HIST2H4 amplification were also compared with those of previously published universal PCRs (28S rRNA, 18S rRNA, and cytochrome b) [18].
• Here, we show that this region of the H4-FO108 gene represents a composite protein-DNA interaction domain for several distinct sequence-specific DNA-binding activities, including HiNF-D, HiNF-M, and HiNF-P [19].
• Tetramers of the arginine-rich histones H3 and H4 associate with supercoiled SV40 DNA either singly, giving tetrameric nucleoprotein complexes or in pairs giving octameric complexes, both of which are visualized as beads in the electron microscope [20].

Analytical, diagnostic and therapeutic context of HIST2H4A

• Chromatin immunoprecipitation assays of the H4/n gene reveal that acetylated histones H3 and H4 are maintained at the same levels in proliferating and postproliferative cells [8].
• H2B and H4 histone mRNA level was assessed with quantitative RT-PCR technique (TaqMan) and histone labeling index (HLI) with in situ hybridization to define proliferation rate, while cytochalasin-block micronucleus assay was performed to measure cytogenetic damage [21].
• SDS-PAGE analysis showed for the recombinant H4 a molecular weight corresponding to the expected one (12,535 Da) [15].
• Characterization of these interactions by various procedures (including affinity chromatography on Pro T alpha-Sepharose columns, immunoblotting assay and investigation of the behaviour of mixtures of Pro T alpha and histones in solution) indicated that Pro T alpha has higher affinity for core histones (particularly H3 and H4) than for H1 [22].

References