Journal article

Publication year: 2002

Pages: 9242-9246

Journal: Journal of Biological Chemistry

Volume number: 277

Issue number: 11

DOI Link: https://doi.org/10.1074/jbc.M110007200

Publisher: Elsevier

Abstract: 

Mammalian Tap-p15 and yeast Mex67p-Mtr2p are conserved and essential
mRNA export factor complexes that transport mRNPs through the nuclear
pore. Here, we report that the small subunit p15 affects the binding of
the large subunit Tap to repeat nucleoporins. BlAcore measurements
revealed that recombinant Tap binds with high affinity (K-d in the nM
range) to repeat nucleoporins and dissociates from them very slowly. In
contrast, when recombinant Tap was bound to p15, the derived
heterodimeric complex exhibited a significant lower affinity to
FG-repeat nucleoporins (K-d in the gm range). Furthermore, when
recombinant Tap lacking the N-terminal nuclear localization sequences
(TapDeltaNLS) was microinjected in mammalian cells, it did not shuttle;
however, TapDeltaNLS with bound p15 efficiently shuttles between nucleus
and cytoplasm. We conclude that heterodimerization of Tap and p15 is
required for shuttling of the functional Tap-p15 mRNA exporter complex.

Harvard Citation style: Katahira, J., Sträßer, K., Saiwaki, T., Yoneda, Y. and Hurt, E. (2002) Complex Formation between Tap and p15 Affects Binding to FG-repeat Nucleoporins and Nucleocytoplasmic Shuttling, Journal of Biological Chemistry, 277(11), pp. 9242-9246. https://doi.org/10.1074/jbc.M110007200

APA Citation style: Katahira, J., Sträßer, K., Saiwaki, T., Yoneda, Y., & Hurt, E. (2002). Complex Formation between Tap and p15 Affects Binding to FG-repeat Nucleoporins and Nucleocytoplasmic Shuttling. Journal of Biological Chemistry. 277(11), 9242-9246. https://doi.org/10.1074/jbc.M110007200