Wu R S, Nishioka D, Bonner W M
J Cell Biol. 1982 May;93(2):426-31. doi: 10.1083/jcb.93.2.426.
The histone 2A proteins of the sea urchin Strongylocentrotus purpuratus are compared with those of the mouse. While the major H2As in these two organisms do not comigrate on two-dimensional gels, the sea urchin contains a protein that comigrates with the minor histone 2A variant H2A.Z from mammals. H2A.Z is of particular interest because its sequence homology with other H2As is quite low, and it is not phosphorylated as are other H2As. A comparison of the tryptic peptide patterns of several H2As from sea urchin blastulae and mouse L1210 cells show that, while the patterns of the H2A.Zs differ greatly from the patterns of the other H2As, the patterns of the mouse and sea urchin H2A.Zs are very similar. Since the H2A.Zs have only one or two peptides in common with the other H2As, the conservation of their sequence indicates that H2A.Zs have evolved under somewhat different selective pressures from other H2As. Unlike all the other sea urchin H2As whose syntheses either turn on or off during early development, H2A.Z seems to be synthesized continuously throughout this period.U
将海胆紫球海胆(Strongylocentrotus purpuratus)的组蛋白2A蛋白与小鼠的组蛋白2A蛋白进行了比较。虽然这两种生物体中的主要H2A蛋白在二维凝胶上不会共同迁移,但海胆含有一种与哺乳动物的次要组蛋白2A变体H2A.Z共同迁移的蛋白质。H2A.Z特别引人关注,因为它与其他H2A的序列同源性相当低,而且不像其他H2A那样被磷酸化。对海胆囊胚和小鼠L1210细胞中几种H2A的胰蛋白酶肽图谱进行比较表明,虽然H