spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Stochaj, U.
Right arrow Articles by Silver, P. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stochaj, U.
Right arrow Articles by Silver, P. A.

Journal of Cell Science, Vol 104, Issue 1 89-95, Copyright © 1993 by Company of Biologists

JOURNAL ARTICLES

Analysis of conserved binding proteins for nuclear localization sequences

U Stochaj, MA Bossie, K van Zee, AM Whalen and PA Silver
Molecular Biology Department, Princeton University, NJ 08544.

Correct targeting of nuclear proteins is mediated by nuclear localization sequences (NLS) which permit specific binding to the nucleus and subsequent translocation across the nuclear envelope via the nuclear pore complex. It is proposed that nuclear import is facilitated by NLS-receptors which reside in the cytoplasm and at the nuclear pore. These NLS-receptors could facilitate an early step of nuclear protein import, i.e. targeting and binding of nuclear proteins at the nuclear pore. We have generated anti-idiotype antibodies against the SV40 T-antigen nuclear localization sequence that allowed us to study NLS-binding proteins in a variety of different organisms. Proteins of similar size are recognized by these antibodies in yeast, Drosophila, rat and human cells. Cytological analysis indicates that the NLS-binding proteins reside in part at nuclear pores. One of the proteins recognized by anti-idiotype antibodies is identical to a previously identified NLS-binding protein. Using isolated yeast nuclei we demonstrate that the anti-idiotype antibodies compete for binding of nuclear proteins in vitro. We show that the yeast mutant npl3, which is defective in nuclear protein localization, has an altered distribution of antigens recognized by these anti-idiotype antibodies, at the semi-permissive temperature. Our results suggest that a set of proteins common to various eukaryotes recognizes nuclear localization sequences.


This article has been cited by other articles:


Home page
 Hum Mol GenetHome page
S. Papin, P. Duquesnoy, C. Cazeneuve, J. Pantel, M. Coppey-Moisan, C. Dargemont, and S. Amselem
Alternative splicing at the MEFV locus involved in familial Mediterranean fever regulates translocation of the marenostrin/pyrin protein to the nucleus
Hum. Mol. Genet., December 1, 2000; 9(20): 3001 - 3009.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
T. D. Sweitzer and J. A. Hanover
Calmodulin activates nuclear protein import: A link between signal transduction and nuclear transport
PNAS, December 10, 1996; 93(25): 14574 - 14579.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
I Cserpan and A Udvardy
The mechanism of nuclear transport of natural or artificial transport substrates in digitonin-permeabilized cells
J. Cell Sci., January 5, 1995; 108(5): 1849 - 1861.
[Abstract] [PDF]

Home page
 J. Cell Sci.Home page
M Vandromme, G Carnac, C Gauthier-Rouviere, D Fesquet, N Lamb, and A Fernandez
Nuclear import of the myogenic factor MyoD requires cAMP-dependent protein kinase activity but not the direct phosphorylation of MyoD
J. Cell Sci., January 2, 1994; 107(2): 613 - 620.
[Abstract] [PDF]


© The Company of Biologists Ltd 1993