| Autor: |
Buss, F, Kent, H, Stewart, M, Bailer, S M, Hanover, J A |
| Zdroj: |
Journal of Cell Science; February 1994, Vol. 107 Issue: 2 p631-8, 8p |
| Abstrakt: |
We have expressed rat nucleoporin p62 cDNA in Escherichia coli to obtain material for structural and self-association studies. Electron microscopy and circular dichroism spectroscopy are consistent with a rod-shaped molecule with an alpha-helical coiled-coil domain at its C terminus and a cross-beta structure at its N terminus, separated by a threonine-rich linker, which has a less-defined secondary structure. Electron microscopy and the solubility properties of fragments produced using thrombin and CNBr digestion indicate that p62 molecules associate to form linear chains and that a small region near the C terminus is an important determinant of assembly. This association may have important consequences for pore structure and function; for example, one way p62 could associate would be to form rings in nuclear pores that could function like barrel hoops. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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