作者: C. Dingwall , S.M. Dilworth , S.J. Black , S.E. Kearsey , L.S. Cox
DOI: 10.1002/J.1460-2075.1987.TB04720.X
关键词:
摘要: Abstract Nucleoplasmin is the most abundant protein in Xenopus oocyte nucleus. It involved histone storage and chromatin assembly it has been used extensively to study transport of proteins into cell We have isolated lambda gt11 phage containing nucleoplasmin cDNA determined sequence entire coding region 200 amino acids for one two genes. The translation product sp6 transcript this same electrophoretic mobility as able form pentamers. shows remarkable clusters charged residues including a long polyglutamic acid tract which presumably constitutes binding site. short C-terminal domain specifies nuclear entry contains four regions are homologous putative localization signals homology migration signal SV40 large T antigen.