Role of different domains in the self-association of rat nucleoporin p62 - PubMed (original) (raw)

. 1994 Feb:107 ( Pt 2):631-8.

doi: 10.1242/jcs.107.2.631.

Affiliations

• PMID: 8207085
• DOI: 10.1242/jcs.107.2.631

Role of different domains in the self-association of rat nucleoporin p62

F Buss et al. J Cell Sci. 1994 Feb.

Abstract

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.

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