Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport.

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. Measureme

SUBMITTER: Lim RY 

PROVIDER: S-EPMC1480438 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature