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

A technique is presented which enables one to measure the extent to which a protein enters and accumulates in the nucleus of the frog oocyte. In this method, the protein, labeled with 125-I, is microinjected into the oocyte. After incubation, the oocyte is manually enucleated and the radioactivity in the nucleus and cytoplasm is determined. Using this technique, proteins lighter than 20,000 daltons were found to enter the nucleus and completely equilibrate between the nucleus and cytoplasm within 24 h. The entry of proteins heavier than 69,000 daltons was severely hindered. Histones and histone fractions entered as quickly as other small proteins, but, in contrast to these proteins, they accumulated in the nucleus to different extents, depending on the total amount of histone injected into the oocyte and the identity of the histone. Evidence is presented that histone fractions compete with each other for accumulation in the nucleus.

Nuclear contents or cytoplasm from Xenopus oocytes labeled with (35-S)methionine or (3-H)proline (donor oocytes) were reinjected into unlabeled oocytes (recipient oocytes). The radioactivity injected as nuclear contents was found to enter and accumulate in the recipient oocyte nucleus. In contrast, the radioactivity injected as cytoplasm was found to enter but not to accumulate in the recipient oocyte nucleus. Sodium dodecyl sulfate (SDS) gel electrophoresis of the nucleus and cytoplasm of donor oocytes revealed the existence of three classes of labeled proteins in these oocytes: those proteins found predominantly in the nucleus (N proteins), those found predominantly in the cytoplasm (C proteins), and those found in both the nucleus and cytoplasm at similar concentrations (B proteins). SDS gel electrophoresis of the nucleus and cytoplasm of recipient oocytes showed that N proteins entered and accumulated in the nucleus but that B proteins partitioned about equally between the nucleus and cytoplasm. A similar analysis of oocytes injected with labeled cytoplasm showed that C proteins did not enter the nucleus but again B proteins partitioned about equally between the nucleus and cytoplasm.