Structural comparisons of mouse histones 2A.X and 2A.Z with 2A.1 and 2A.2.
The tryptic peptide patterns of the recently described H2A species H2A.X and H2A.Z from mouse were compared with the tryptic peptide patterns of the major mouse H2A's, H2A.1 and H2A.2. The identities of the H2A.1 peptides were determined by comparing their in vivo labeling with various 14C-labeled amino acids with the expected labeling determined from the known sequence. All the H2A.1 tryptic peptides larger than dipeptides were accounted for. The procedure was repeated for H2A.2, H2A.X and H2A.Z. H2A.X was found to have large regions of sequence identical to that of H2A.1 with the variability occurring mainly near the N and C termini. Mouse H2A.X had some sequence characteristics found in the sequenced H2A's of trout and sea urchin. In contrast, H2A.Z was found to have only two peptides in common with H2A.1; in addition, the labeling patterns of the non-identical peptides were too different to suggest analogous peptides. We conclude from these studies that H2A.Z differs considerably from H2A.1 in major portions of its sequence.
D000595:Amino Acid Sequence; D000818:Animals; D006657:Histones / Q000302:isolation & purification; D007939:Leukemia L1210 / Q000378:metabolism; D051379:Mice; D010446:Peptide Fragments / Q000032:analysis; D012617:Sea Urchins; D013045:Species Specificity; D013329:Structure-Activity Relationship; D014337:Trout; D014357:Trypsin
D006657:Histones; D010446:Peptide Fragments; D014357:Trypsin