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- W82168767 abstract "Research Article1 May 1989free access Nuclear transport kinetics depend on phosphorylation-site-containing sequences flanking the karyophilic signal of the Simian virus 40 T-antigen. H. P. Rihs H. P. Rihs Max-Planck-Institut für Biophysik, Frankfurt, FRG. Search for more papers by this author R. Peters R. Peters Max-Planck-Institut für Biophysik, Frankfurt, FRG. Search for more papers by this author H. P. Rihs H. P. Rihs Max-Planck-Institut für Biophysik, Frankfurt, FRG. Search for more papers by this author R. Peters R. Peters Max-Planck-Institut für Biophysik, Frankfurt, FRG. Search for more papers by this author Author Information H. P. Rihs1 and R. Peters1 1Max-Planck-Institut für Biophysik, Frankfurt, FRG. The EMBO Journal (1989)8:1479-1484https://doi.org/10.1002/j.1460-2075.1989.tb03531.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Selective nuclear protein transport was analyzed in single living cells. Hybrid proteins consisting of short stretches of the Simian virus 40 T-antigen and of the almost complete beta-galactosidase moiety were generated by molecular genetic methods and injected into the cytoplasm of rodent hepatoma cells. A histochemical assay showed that all proteins containing the karyophilic signal of the T-antigen (residues 126/127-132) were equally well accumulated by the nucleus within 15 h after injection. Microfluorimetric measurements of nuclear transport kinetics, however, revealed large differences. Proteins containing the karyophilic signal without flanking sequences were taken up by the nucleus on a time scale of hours. The same held for a protein containing T-antigen residues 127-147. However, a protein containing T-antigen residues 111-135 was accumulated by the nucleus with a half-time of 8-10 min reaching an equilibrium nucleocytoplasmic concentration ratio of greater than or equal to 15. Photobleaching measurements showed that, independently of subcellular localization, the mobility of all proteins was quite large. Thus, our measurements revealed a striking effect of T-antigen residues 111-125 on the kinetics of nuclear transport. Residues 111-125 do not seem to contain a second karyophilic signal. Conspicuously, however, they comprise a cluster of phosphorylation sites. Previous ArticleNext Article Volume 8Issue 51 May 1989In this issue RelatedDetailsLoading ..." @default.
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- W82168767 title "Nuclear transport kinetics depend on phosphorylation-site-containing sequences flanking the karyophilic signal of the Simian virus 40 T-antigen." @default.
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