Disease relevance of HIST2H2BE

• Association of antibody to histone complex H2A-H2B with symptomatic procainamide-induced lupus [1].
• Weak reactivity with H2B and H4 were also found in three sera from the patients with polymyositis/dermatomyositis [2].
• Histone H2B mRNA level and HLI may be a useful molecular predictor of the tumour response to radiation treatment in gliomas of the same histological grade, however the risk of potentially more rapid tumour-cell repopulation must be considered [3].
• Cell proliferative activity estimated by histone H2B mRNA level correlates with cytogenetic damage induced by radiation in human glioblastoma cell lines [3].
• Natural macromolecular polycations (protamine, histones H1, H2A, H2B and H3) caused the clustering of influenza and parainfluenza viruses into aggregates heterogeneous in size, as well as a decrease in their hemagglutinating capacity [4].

High impact information on HIST2H2BE

• Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II [5].
• Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase [6].
• These studies thus link the H2B transcriptional machinery to cell cycle regulators, and possibly to cellular metabolic state (redox status), and set the stage for studies of the underlying mechanisms and the basis for coordinated histone gene expression and coupling to DNA replication [7].
• Furthermore, the octamer domains of the adenovirus DNA replication origin, the histone H2B, and the immunoglobulin light chain genes bound and competed for TRF [8].
• In DNAase I protection experiments, the CCAAT-binding factor of only the testis extract is able to interact with the sperm H2B promoter [9].

Biological context of HIST2H2BE

• We propose that the docking of RCC1 to H2A/H2B establishes the polarity of the Ran-GTP gradient that drives nuclear envelope assembly, nuclear transport, and other nuclear events [10].
• In yeast, histone H2B monoubiquitination is a cotranscriptional event regulating histone H3 methylation at lysines 4 and 79 [11].
• RNF20 overexpression leads to elevated H2B monoubiquitination, subsequently higher levels of methylation at H3 lysines 4 and 79, and stimulation of HOX gene expression [11].
• We propose a model in which phosphorylation/dephosphorylation regulates chaperoning of H2B by hsp60 in the plasma membrane [12].
• Ten human/mouse hybrid cell lines that segregate either human or mouse chromosomes were examined for the expression of human- and mouse-specific histones H1 and H2B [13].

Anatomical context of HIST2H2BE

• Isolation and characterization of a cDNA from a human histone H2B gene which is reciprocally expressed in relation to replication-dependent H2B histone genes during HL60 cell differentiation [14].
• Stable HeLa cell lines expressing histones H2B, H3, and H4 tagged with green fluorescent protein (GFP) were established; the tagged molecules were assembled into nucleosomes [15].
• 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 [16].
• 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 [17].
• One form of H2A and one form of H2B are synthesized only during the period from fertilization to the blastula stage [18].

Associations of HIST2H2BE with chemical compounds

• Eight histones (H1-1, H1-2, H2A-1, H2A-2, H2B, H3-1, H3-2, H4) were separated on a C4 stationary phase with complete resolution, never reached in previous HPLC-MS methods, by using a gradient elution with the combined presence of heptafluorobutyric acid and formic acid as acidic modifiers in the mobile phase [19].
• The rapidly exchanging fraction disappeared in 5,6-dichloro-1-beta-d-ribofuranosylbenzimidazole and so may represent H2B in transcriptionally active chromatin [15].
• The strongest determinant on H1 was located within the COOH-terminal half, with a weaker determinant being present within the NH2-terminal half; the H2B determinant(s) was located entirely within the NH2-terminal half of the molecule [20].
• Incubation of ADP-ribose with histones H1, H2A, H2B, and H4 at pH 7.5 resulted in the formation of ketoamine glycation conjugates [21].
• CRP binding to the H2A-H2B dimer and (H3-H4)2 tetramer was demonstrated and these reactions were inhibited by phosphocholine [22].

Physical interactions of HIST2H2BE

• Mechanistic studies revealed that the human INO80 complex catalyzes nucleosome sliding and the SRCAP complex catalyzes ATP-dependent exchange of histone H2A/H2B dimers containing the histone variant H2A.Z into nucleosomes [23].

Regulatory relationships of HIST2H2BE

• Formation of a trimeric complex with hPAF stimulates H2B monoubiquitination activity in vitro [11].
• Moreover, Mdm2 induces H2B monoubiquitylation in vivo [24].

Other interactions of HIST2H2BE

• Hsp60 physically associated with H2B when both molecules were in their dephospho forms [12].
• An unusual feature of the spacer region between the H4 and H2B genes is the presence of a duplicated sequence 87 bp in length [25].
• The human histone proteins that were characterized were H3.3A histone (NCBI accession number: 51859376), H2B histone (NCBI accession number: 1568557), H2A.5 histone (NCBI accession number: 70686), H1 (NCBI accession number: 22770677), and H2.1 histone (SwissProt accession number: P16403) [26].
• Variable region genes of human monoclonal autoantibodies to histones H2A and H2B from a systemic lupus erythematosus patient [27].
• The mRNA Export Factor Sus1 Is Involved in Spt/Ada/Gcn5 Acetyltransferase-mediated H2B Deubiquitinylation through Its Interaction with Ubp8 and Sgf11 [28].

Analytical, diagnostic and therapeutic context of HIST2H2BE

• Northern blot analysis indicated that the levels of the 2300-nt HHC289 mRNA species did not vary significantly during the HeLa S3 cell cycle, in comparison to replication-dependent H2B mRNAs which are elevated 15-fold during S phase [14].
• The H2B-GL105 histone gene was localized to chromosome region 1q21-1q23 by chromosomal in situ hybridization and by analysis of rodent-human somatic cell hybrids using an H2B-GL105 specific probe [29].
• Separate determinants on H1 and H2B were demonstrated by immunoblotting with affinity-purified anti-H1 and anti-H2B antibodies derived from serum that showed both specificities [20].
• Further amino-terminal sequence analyses point to a high-scoring relationship in this region to histone sequences, namely, histone H2B, but to no published sequences for any heparin-binding growth factor [16].
• Further purification of histones H2A, H2B, and H4 by reversed-phase HPLC also yielded a tetrahydrotetrol of benzo[a]pyrene, indicating that these three histones had some labile adducts [30].

References