English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Systematic analysis of barrier-forming FG hydrogels from Xenopus nuclear pore complexes.

Labokha, A., Gradmann, S., Frey, S., Hülsmann, B. B., Urlaub, H., Baldus, M., et al. (2013). Systematic analysis of barrier-forming FG hydrogels from Xenopus nuclear pore complexes. EMBO Journal, 32(2), 204-218. doi:10.1038/emboj.2012.302.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-DFD8-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-C8CF-3
Genre: Journal Article

Files

show Files
hide Files
:
1694076-Suppl.pdf (Supplementary material), 2MB
Name:
1694076-Suppl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-

Creators

show
hide
 Creators:
Labokha, A.1, Author              
Gradmann, S., Author
Frey, S.1, Author              
Hülsmann, B. B.1, Author              
Urlaub, H.2, Author              
Baldus, M., Author
Görlich, D.1, Author              
Affiliations:
1Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society, ou_578574              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

Content

show
hide
Free keywords: exportin; FG hydrogel; importin; nuclear pore complex; O-glycosylation
 Abstract: Nuclear pore complexes (NPCs) control the traffic between cell nucleus and cytoplasm. While facilitating translocation of nuclear transport receptors (NTRs) and NTR·cargo complexes, they suppress passive passage of macromolecules greater than or equal to30 kDa. Previously, we reconstituted the NPC barrier as hydrogels comprising S. cerevisiae FG domains. We now studied FG domains from 10 Xenopus nucleoporins and found that all of them form hydrogels. Related domains with low FG motif density also substantially contribute to the NPC’s hydrogel mass. We characterized all these hydrogels and observed the strictest sieving effect for the Nup98-derived hydrogel. It fully blocks entry of GFP-sized inert objects, permits facilitated entry of the small NTR NTF2, but arrests importin β-type NTRs at its surface. O-GlcNAc modification of the Nup98 FG domain prevented this arrest and allowed also large NTR·cargo complexes to enter. Solid-state NMR spectroscopy revealed that the O-GlcNAc-modified Nup98 gel lacks amyloid-like β-structures that dominate the rigid regions in the S. cerevisiae Nsp1 FG hydrogel. This suggests that FG hydrogels can assemble through different structural principles and yet acquire the same NPC-like permeability.

Details

show
hide
Language(s): eng - English
 Dates: 2012-11-302013-01-23
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/emboj.2012.302
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: EMBO Journal
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 32 (2) Sequence Number: - Start / End Page: 204 - 218 Identifier: -