Disease relevance of HIST2H2AC

• H2A and H4 were digested with Staphylococcus aureus V8 protease, and the digests were separated by RP-HPLC [1].
• Association of antibody to histone complex H2A-H2B with symptomatic procainamide-induced lupus [2].
• In the present study, we focused on the relationship between the ubiquitination status of histone H2A, the structure of chromatin, and the efficiency of nucleotide excision repair (NER) of cisplatin-DNA adducts in human ovarian carcinoma cells exposed to the antitumor drug cisplatin [3].
• The antisera also contained IgG antibodies which bound components that correspond to common target antigens in autoimmune diseases such as native dsDNA, peptides of Sm-D antigen, ubiquitin, branched peptides of ubiquitinated H2A and poly(ADP-ribose) [4].
• These results indicate that the AC inhibitor in the pancreatic cancer extract is histone H1b or H1d and histones H2A, H2B and H3 also have an AC inhibitory activity [5].

High impact information on HIST2H2AC

• In this issue of Cell, Meneghini et al. demonstrate that replacement of canonical histone H2A with the histone variant H2A.Z within euchromatin prevents silent chromatin proteins from migrating into regions of the chromosome that normally are transcriptionally active [6].
• We have studied the exact sequence requirement for the formation of 3' termini of the sea urchin H2A mRNA in frog oocyte injection experiments [7].
• The coding regions of these two histone gene variants share considerable sequence homology; however, there are areas of nonhomology in every spacer region and the lengths of the nonhomologous spacers between the H2A and H1 genes are not the same for the two repeat unit classes (inter-gene heterogeneity) [8].
• They deposit variant H2A and H3 histones and are targeted to particular functional sites in the genome [9].
• It has recently been shown that the histone H2A variant H2AX specifically controls the recruitment of DNA repair proteins to the sites of DNA damage [10].

Chemical compound and disease context of HIST2H2AC

• Finally, the H2A sns fragment placed between the simian virus 40 regulative region and the tk promoter repressed chloramphenicol acetyltransferase expression in transfected human cell lines [11].
• The effect of a polycation (histone H2A) and of oligocations (spermine, spermidine and putrescine) on Sendai and influenza virus particles was investigated by light scattering measurements at 90 degrees and at various wavelengths [12].
• As evaluated by light scattering at 90 degrees, natural organic oligocations such as putrescine, spermidine and spermine interfered with myxovirus aggregates which were induced by the histone H2A and strongly amplified by shaking during incubation [13].
• In contrast, the synthetic oligocation 1.7-diamino heptane itself aggregated the virus particles, its action being unmodified by adding polycationic H2A in abundance [13].

Biological context of HIST2H2AC

• These studies reveal that NHK-1-catalyzed phosphorylation of a conserved serine/threonine residue in H2A is a new component of the histone code that might be related to cell cycle progression [14].
• Phosphorylation of histone H2A inhibits transcription on chromatin templates [15].
• Modifications in the H2A histone degree of acetylation were revealed by treatment of the cells with butyrate (H2A-1, H2A-2) and valproate (H2A-2) [16].
• Collectively, these studies have identified five novel biotinylation sites in human histones; histone H2A is unique among histones in that its biotinylation sites include amino acid residues from the C-terminus [17].
• This unequivocal identification of H2A forms illustrates the advantages of Top Down Mass Spectrometry and provides a global perspective of H2A regulation through the cell cycle [18].

Anatomical context of HIST2H2AC

• Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes [1].
• Top Down analysis revealed that at least fourteen genes encoding histone H2A are coexpressed in HeLa cells [18].
• Calculation of relatedness on the basis of differences in amino acid composition corroborates the conclusion of molecular distinction between the lectin, histones H2A and H2B, and the fibroblast growth factor as well as angiogenin [19].
• Using human cell lines, we have analyzed the expression patterns of functional human H2A/H2B gene pairs organized within the two histone gene clusters on the short arm of chromosome 6 [20].
• Not only histone H1 but also histones H2A, H2B and H3 from calf thymus inhibited AC activity [5].

Associations of HIST2H2AC with chemical compounds

• Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase [17].
• CRP binding to the H2A-H2B dimer and (H3-H4)2 tetramer was demonstrated and these reactions were inhibited by phosphocholine [21].
• Incubation of ADP-ribose with histones H1, H2A, H2B, and H4 at pH 7.5 resulted in the formation of ketoamine glycation conjugates [22].
• We isolated the histone H2A-H2B gene pair as a copy-number suppressor of sonB1 cold sensitivity and hydroxyurea sensitivity [23].
• Compared with those os S. cerevisiae and human, variable residues were clustered near the NH2- and COOH-terminal regions of H2A and H2B [24].

Physical interactions of HIST2H2AC

• We find that RCC1 binds directly to mononucleosomes and to histones H2A and H2B [25].
• The NC2 subunits dimerize and bind to TATA binding protein (TBP)-promoter complexes via histone fold domains of the H2A-H2B type [26].
• The data are consistent with a model in which remodeling results in the unraveling of a region of DNA from the edge of the nucleosome, leading to a repositioning of the H2A/H2B dimer to a noncanonical position near the center of the remodeled complex [27].

Other interactions of HIST2H2AC

• Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B [25].
• Interaction with hTAF(II)20 requires a domain of hTAF(II)135 which shows sequence homology to H2A [28].
• This result indicates that transcribing RNA polymerase II remodels chromatin in part through coincident displacement of H2A.Z-H2B dimers and incorporation of H2A-H2B dimers [29].
• The H2A variants present in sperm (H2A.X and limited H2A.Z) have been shown previously to be minor variants in somatic chromatin [30].
• Tying C' ends of H2A and H2B using a molecular glue, tissue-type transglutaminase [31].

Analytical, diagnostic and therapeutic context of HIST2H2AC

• N-terminal sequence analysis of the 16 and 18 kDa proteins and of a tryptic fragment of the protein mixture revealed strong homologies with deduced cDNA or protein sequences of histones H2A, H2B, and H3 of P. falciparum and other species [32].
• Pulse-chase kinetics suggested that both ubiquitin thiol esters formed to E2(20kDa) were catalytically competent in H2A ligation [33].
• The kinetic folding mechanism for the H2A/H2B dimer has been determined from unfolding and refolding kinetics as a function of urea using stopped-flow, circular dichroism and fluorescence methods [34].
• Peptide mapping and amino acid analysis of radiolabelled CS H2A showed that phosphorylation occurred mainly on serine residues located in the C-terminal region of the molecule [35].
• H2A-H2B dimer fractions obtained from MH-134SC cells labeled with suitable precursors were fractionated by rate zonal centrifugation in sucrose gradients containing 2 M NaCl [36].

References