The gene encoding Xenopus B-Myb (XB-Myb), a protein structurally relat
ed to the nuclear protooncogene product c-Myb, is expressed in early X
enopus embryogenesis. We report on developmental alterations in the nu
cleocytoplasmic distribution and phosphorylation of XB-Myb in Xenopus
oocytes and embryos, as well as on a negative regulatory role of the c
arboxyl terminus in sequence specific DNA binding. In growing oocytes
and early embryonic stages the protein is primarily located in the nuc
leus; in the full-grown oocyte, however, it remains sequestered in the
cytoplasmic compartment. Upon meiotic maturation of the oocyte, XB-My
b becomes hyperphosphorylated. Oocyte/egg isolates of XB-Myb are inhib
ited in their specific DNA binding activity; truncation of the carboxy
l terminal region relieves this block in nucleic acid recognition. Fur
thermore, we have used overexpression of XB-Myb in Xenopus embryos by
means of mRNA injection as an assay for gene function in vivo. Overexp
ression of full-length XB-Myb, not of the carboxyl terminal deletion m
utant, results in an altered morphology of lateral plate mesoderm.