Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: binding of nucleoporin p54 to the rod domain of p62

doi:10.1083/jcb.128.3.251

This Article

	Full Text (PDF, 2292K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Buss, F.
	Articles by Stewart, M.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Buss, F.
	Articles by Stewart, M.


Social Bookmarking

	What's this?

ARTICLES

Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: binding of nucleoporin p54 to the rod domain of p62

F Buss and M Stewart
Medical Research Council Laboratory of Molecular Biology, Cambridge, England.

Nuclear pore complexes are constructed from a large number of different proteins, called collectively nucleoporins. One of these nucleoporins, p62, has an alpha-helical coiled-coil COOH-terminal rod domain linked to an NH2-terminal domain that contains a series of degenerate pentapeptide repeats. In nuclear pores p62 forms a tight complex with at least two other proteins, p58 and p54, which can be extracted from isolated rat liver nuclei (Finlay, D. R., E. Meier, P. Bradley, J. Horecka, and D. J. Forbes. 1991. J. Cell Biol. 114:169-183). We have used a range of methods to demonstrate a strong binding between p62 and p54 in this complex and show that the rod domain of p62 appears to constitute the principal binding site for p54. Whole p62 and its rod domain expressed in Escherichia coli both bind strongly to p54 in blot- overlay assays. Most of the epitopes on the p62 rod recognized by polyclonal antisera are masked in the complex, whereas epitopes on the NH2-terminal domain of p62 are still exposed, both in the isolated complex and also in nuclear pores stained in situ by immunofluorescence in isolated rat nuclei. Moreover, it has been possible to exchange recombinant p62 rod for some of the native p62 in complexes partially dissociated by 4 M urea. Overall these results suggest a key role for the p62 rod domain in maintaining the structural integrity of the complex and also suggest a molecular model for the complex. This model is consistent with data that indicate that the analogous coiled-coil region of yeast nucleoporin NSP1 may function in a similar way.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Feldherr, C., Akin, D., Littlewood, T., Stewart, M. (2002). The molecular mechanism of translocation through the nuclear pore complex is highly conserved. J. Cell Sci. 115: 2997-3005 [Abstract] [Full Text]
Bailer, S. M., Balduf, C., Hurt, E. (2001). The Nsp1p Carboxy-Terminal Domain Is Organized into Functionally Distinct Coiled-Coil Regions Required for Assembly of Nucleoporin Subcomplexes and Nucleocytoplasmic Transport. Mol. Cell. Biol. 21: 7944-7955 [Abstract] [Full Text]
Elton, D., Simpson-Holley, M., Archer, K., Medcalf, L., Hallam, R., McCauley, J., Digard, P. (2001). Interaction of the Influenza Virus Nucleoprotein with the Cellular CRM1-Mediated Nuclear Export Pathway. J. Virol. 75: 408-419 [Abstract] [Full Text]
Shah, S., Tugendreich, S., Forbes, D. (1998). Major Binding Sites for the Nuclear Import Receptor Are the Internal Nucleoporin Nup153 and the Adjacent Nuclear Filament Protein Tpr. JCB 141: 31-49 [Abstract] [Full Text]
Lu, D., Yang, H., Raizada, M. K. (1998). Involvement of p62 Nucleoporin in Angiotensin II-Induced Nuclear Translocation of STAT3 in Brain Neurons. J. Neurosci. 18: 1329-1336 [Abstract] [Full Text]
Iborra, F., Jackson, D., Cook, P. (1998). The path of transcripts from extra-nucleolar synthetic sites to nuclear pores: transcripts in transit are concentrated in discrete structures containing SR proteins. J. Cell Sci. 111: 2269-2282 [Abstract]
Grandi, P., Dang, T., Pané, N., Shevchenko, A., Mann, M., Forbes, D., Hurt, E. (1997). Nup93, a Vertebrate Homologue of Yeast Nic96p, Forms a Complex with a Novel 205-kDa Protein and Is Required for Correct Nuclear Pore Assembly. Mol. Biol. Cell 8: 2017-2038 [Abstract] [Full Text]
Bastos, R., Pouplana, L. R. d., Enarson, M., Bodoor, K., Burke, B. (1997). Nup84, A Novel Nucleoporin That Is Associated With CAN/Nup214 on the Cytoplasmic Face of the Nuclear Pore Complex. JCB 137: 989-1000 [Abstract] [Full Text]