## Abstract Divalent metal transporter 1 (DMT1; also called __DCT1__, __Nramp2__, or __SLC11A2__) has multiple isoforms that localize differently in many cell types. DMT1 +IRE species (encoded by mRNA with an iron‐responsive element) are limited to the plasma membrane and cytosolic vesicles. In neu
Nuclear transport of H1 histones meets the criteria of a nuclear localization signal—mediated process
✍ Scribed by M. Kurz; D. Doenecke; W. Albig
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 165 KB
- Volume
- 64
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
We have studied the nuclear transport of H1 histones using the digitonin permeabilization assay system in order to establish the transport requirements for H1 translocation to the nucleus. Using HeLa cells and fluorescencelabeled calf thymus H1, we show that the H1 nuclear transport in permeabilized cells requires the addition of cytoplasmic extract. Furthermore, it can be blocked by energy depletion and by chilling or by addition of wheat germ agglutinin or by nonhydrolyzable GTP analogs. Thus, the import of H1 histones follows the criteria established for nuclear import mediated by nuclear localization signals (NLS). The distribution of basic amino acids in average H1 sequences, however, does not allow the assignment of a specific element as a classical NLS.
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