The conserved amino-terminal domain of hSRP1 alpha is essential for nuclear protein import.
作者： K. Weis , U. Ryder , A. I. Lamond
DOI: 10.1002/J.1460-2075.1996.TB00531.X
关键词: Conserved sequence 、 Importin-alpha 、 Biology 、 Nuclear protein 、 Biochemistry 、 Nuclear pore 、 Alpha Karyopherins 、 Cell biology 、 Transport protein 、 Nuclear localization sequence 、 Nuclear transport
摘要: Nuclear proteins are targeted through the nuclear pore complex (NPC) in an energy-dependent reaction. The import reaction is mediated by localization sequences (NLS) substrate which recognized heterodimeric cytoplasmic receptors. hSRP1 alpha NLS-binding subunit of human NLS receptor and complexed vivo with a second 97 kDa (p97). We show here that short amino-terminal domain necessary sufficient for its interaction p97. This conserved other SRP1-like fusion to reporter protein promote complete import, circumventing usual requirement interaction. same inhibits NLS-containing when added vitro transport assay. While full-length hSRP able leave nucleus, alone not exit. conclude functions as adaptor tether substrates machinery.
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