| Literature DB >> 8001116 |
D Görlich1, S Prehn, R A Laskey, E Hartmann.
Abstract
We have purified a cytosolic protein from Xenopus eggs that is essential for selective protein import into the cell nucleus. The purified protein, named importin, promotes signal-dependent binding of karyophilic proteins to the nuclear envelope. We have cloned, sequenced, and expressed a corresponding cDNA. Importin shows 44% sequence identity with SRP1p, a protein associated with the yeast nuclear pore complex. Complete, signal-dependent import into HeLa nuclei can be reconstituted by combining importin purified from Xenopus eggs or expressed in E. coli with Ran/TC4. Evidence for additional stimulatory factors is provided.Entities:
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Year: 1994 PMID: 8001116 DOI: 10.1016/0092-8674(94)90067-1
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582