High impact information on H2A-IX

• Histone H2A ubiquitination is a bulky posttranslational modification that occurs at the vicinity of the binding site for linker histones in the nucleosome [1].
• Histone H2A ubiquitination does not preclude histone H1 binding, but it facilitates its association with the nucleosome [1].
• The MgCl2-induced folding of defined 12-mer nucleosomal arrays, in which ubiquitinated histone H2A (uH2A) replaced H2A, was analyzed by quantitative agarose gel electrophoresis and analytical centrifugation [2].
• The most dramatic effect was seen in the rapid disappearance of the ubiquitinated form of histone H2A, one of the major ubiquitin conjugates in cells in the interphase portion of their growth cycle [3].
• The DNA sequence of a chicken genomal fragment containing a histone H2A gene has been determined [4].

Biological context of H2A-IX

• It contains extensive 5' and 3' flanking regions and encodes a protein identical in sequence to the histone H2A protein isolated from chicken erythrocytes [4].
• Changes in nuclear content of protein conjugate histone H2A-ubiquitin during rooster spermatogenesis [5].
• The complete amino acid sequence (128 residues) of the chicken erythrocyte histone H2A was deduced from the data provided by structural studies on the tryptic peptides from the maleylated histone and of the peptides obtained by thermolysin digestion of the native protein [6].
• A chicken histone H2A probe has been used to isolate five different clones from a mouse genomic library in lambda Charon 4A [7].

Anatomical context of H2A-IX

• Ubiquitinated and diubiquitinated histone H2A remained at similar levels in early and late stage testis nucleohistone [8].
• In addition, modulation of variant synthesis within the histone H2A and H3 classes may accompany myotube formation [9].
• Its binding to fibronectin was approximately twice the binding of [32P] labelled wild type lambda, where as binding to control of equimolar concentration of calf thymus histone H 2 A was approximately equal [10].

Associations of H2A-IX with chemical compounds

• It is suggested that the nucleophilic target amino acid for BPDE-I binding in histone H2A may be a histidine located close to the C terminus [11].

Analytical, diagnostic and therapeutic context of H2A-IX

• This result was confirmed by HPLC analyses of V8-protease digests of BPDE-I bound to histone H2A purified from the three different nuclei [11].
• Antisera raised against eight synthetic, unconjugated peptides all reacted with histone H2A in ELISA [12].

References