caa a22 4500 475774590 CHVBK 20180406123627.0 cr unu---uuuuu 170329e20000601xx s 000 0 eng 10.1007/s004180000147 doi (NATIONALLICENCE)springer-10.1007/s004180000147 Langer Thomas Institut für Biochemie der Johann Wolfgang Goethe-Universität Frankfurt am Main, Marie Curie Strasse 9, 60439 Frankfurt am Main, Germany aut Nuclear transport of histone2b in mammalian cells is signal- and energy-dependent and different from the importin α/β-mediated process [Elektronische Daten] [Thomas Langer] Abstract.: Histone2b nuclear transport was investigated using the digitonin-permeabilized cell system and the rat liver resealed nuclear envelope system. In permeabilized cells, maximal uptake of histone2b is dependent on cytosolic components and an appropriate energy source. Addition of the recombinant proteins importinα/β, and Ran, as well as ATP and GTP, to cytosol-depleted permeabilized cells does not enhance the uptake of histone2b in contrast to that of nucleoplasmin serving as a control. Nuclear import of histone2b cannot be blocked by addition of an excess of a nuclear localization signal-bearing peptide or nucleoplasmin. Similar results were obtained with resealed nuclear envelopes. As shown previously, resealed vesicles respond to the importin signal for the uptake of nuclear localization signal-bearing proteins which allows investigation of the import mechanism independent of intranuclear binding to chromatin. Uptake of histone2b therefore seems to be an energy-requiring transport mechanism different from the import of proteins bearing a typical nuclear localization signal. Springer-Verlag, 2000 Nuclear transport Histone Importin Nuclear envelope nationallicence https://doi.org/10.1007/s004180000147 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s004180000147 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Langer Thomas Institut für Biochemie der Johann Wolfgang Goethe-Universität Frankfurt am Main, Marie Curie Strasse 9, 60439 Frankfurt am Main, Germany aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer