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Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport

Lim, Roderick Y. H. and Huang, Ning-Ping and Köser, Joachim and Deng, Jie and Lau, K. H. Aaron and Schwarz-Herion, Kyrill and Fahrenkrog, Birthe and Aebi, Ueli. (2006) Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proceedings of the National Academy of Sciences of the United States of America, 103 (25). pp. 9512-9517.

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Official URL: http://edoc.unibas.ch/dok/A5259689

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Abstract

Natively unfolded phenylalanine-glycine (FG)-repeat domains are alleged to form the physical constituents of the selective barrier-gate in nuclear pore complexes during nucleocytoplasmic transport. Presently, the biophysical mechanism behind the selective gate remains speculative because of a lack of information regarding the nanomechanical properties of the FG domains. In this work, we have applied the atomic force microscope to measure the mechanical response of individual and clusters of FG molecules. Single-molecule force spectroscopy reveals that FG molecules are unfolded and highly flexible. To provide insight into the selective gating mechanism, an experimental platform has been constructed to study the collective behavior of surface-tethered FG molecules at the nanoscale. Measurements indicate that the collective behavior of such FG molecules gives rise to an exponentially decaying long-range steric repulsive force. This finding indicates that the molecules are thermally mobile in an extended polymer brush-like conformation. This assertion is confirmed by observing that the brush-like conformation undergoes a reversible collapse transition in less polar solvent conditions. These findings reveal how FG-repeat domains may simultaneously function as an entropic barrier and a selective trap in the near-field interaction zone of nuclear pore complexes; i.e., selective gate.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Aebi)
05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Fahrenkrog)
05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nanobiology Argovia (Lim)
UniBasel Contributors:Lim, Roderick Y.H. and Aebi, Ueli and Fahrenkrog, Birthe
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:National Academy of Sciences
ISSN:0027-8424
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
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Last Modified:10 Apr 2018 14:21
Deposited On:22 Mar 2012 13:23

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