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Elife. 2015 Sep 15;4. pii: e10027. doi: 10.7554/eLife.10027.

The molecular mechanism of nuclear transport revealed by atomic-scale measurements.

Author information

1
The Rockefeller University, New York, United States.
2
New York Structural Biology Center, New York, United States.
3
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, United States.

Abstract

Nuclear pore complexes (NPCs) form a selective filter that allows the rapid passage of transport factors (TFs) and their cargoes across the nuclear envelope, while blocking the passage of other macromolecules. Intrinsically disordered proteins (IDPs) containing phenylalanyl-glycyl (FG)-rich repeats line the pore and interact with TFs. However, the reason that transport can be both fast and specific remains undetermined, through lack of atomic-scale information on the behavior of FGs and their interaction with TFs. We used nuclear magnetic resonance spectroscopy to address these issues. We show that FG repeats are highly dynamic IDPs, stabilized by the cellular environment. Fast transport of TFs is supported because the rapid motion of FG motifs allows them to exchange on and off TFs extremely quickly through transient interactions. Because TFs uniquely carry multiple pockets for FG repeats, only they can form the many frequent interactions needed for specific passage between FG repeats to cross the NPC.

KEYWORDS:

S. cerevisiae; biophysics; cell biology; nuclear magnetic resonance; nuclear pore; nucleoporins; structural biology; transport factors

PMID:
26371551
PMCID:
PMC4621360
DOI:
10.7554/eLife.10027
[Indexed for MEDLINE]
Free PMC Article

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