Abstract
The largely intrinsically disordered phenylalanine-glycine-rich nucleoporins (FG Nups) underline a selectivity mechanism that enables the rapid translocation of transport factors (TFs) through the nuclear pore complexes (NPCs). Conflicting models of NPC transport have assumed that FG Nups undergo different conformational transitions upon interacting with TFs. To selectively characterize conformational changes in FG Nups induced by TFs we performed small-angle neutron scattering (SANS) with contrast matching. Conformational-ensembles derived from SANS data indicated an increase in the overall size of FG Nups is associated with TF interaction. Moreover, the organization of the FG motif in the interacting state is consistent with prior experimental analyses defining that FG motifs undergo conformational restriction upon interacting with TFs. These results provide structural insights into a highly dynamic interaction and illustrate how functional disorder imparts rapid and selective FG Nup-TF interactions. Sparks et al. use small-angle neutron scattering experiments to describe the fuzzy interactions between disordered FG Nups and transport factors (TFs) from the nuclear pore complex, thus elucidating the subtle conformational changes that TFs induce within FG Nup chains. The study helps to define "fuzziness" at intermediate length scales.
| Original language | English (US) |
|---|---|
| Journal | Structure |
| DOIs | |
| State | Accepted/In press - Jan 1 2018 |
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Keywords
- Contrast matching
- Ensemble analysis
- FG nucleoporins
- Intrinsically disordered proteins
- Kap95
- NTF2
- Nuclear pore complex
- Nuclear transport
- Small-angle neutron scattering
- Transport factors
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
Cite this
Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering. / Sparks, Samuel; Temel, Deniz B.; Rout, Michael P.; Cowburn, David.
In: Structure, 01.01.2018.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering
AU - Sparks, Samuel
AU - Temel, Deniz B.
AU - Rout, Michael P.
AU - Cowburn, David
PY - 2018/1/1
Y1 - 2018/1/1
N2 - The largely intrinsically disordered phenylalanine-glycine-rich nucleoporins (FG Nups) underline a selectivity mechanism that enables the rapid translocation of transport factors (TFs) through the nuclear pore complexes (NPCs). Conflicting models of NPC transport have assumed that FG Nups undergo different conformational transitions upon interacting with TFs. To selectively characterize conformational changes in FG Nups induced by TFs we performed small-angle neutron scattering (SANS) with contrast matching. Conformational-ensembles derived from SANS data indicated an increase in the overall size of FG Nups is associated with TF interaction. Moreover, the organization of the FG motif in the interacting state is consistent with prior experimental analyses defining that FG motifs undergo conformational restriction upon interacting with TFs. These results provide structural insights into a highly dynamic interaction and illustrate how functional disorder imparts rapid and selective FG Nup-TF interactions. Sparks et al. use small-angle neutron scattering experiments to describe the fuzzy interactions between disordered FG Nups and transport factors (TFs) from the nuclear pore complex, thus elucidating the subtle conformational changes that TFs induce within FG Nup chains. The study helps to define "fuzziness" at intermediate length scales.
AB - The largely intrinsically disordered phenylalanine-glycine-rich nucleoporins (FG Nups) underline a selectivity mechanism that enables the rapid translocation of transport factors (TFs) through the nuclear pore complexes (NPCs). Conflicting models of NPC transport have assumed that FG Nups undergo different conformational transitions upon interacting with TFs. To selectively characterize conformational changes in FG Nups induced by TFs we performed small-angle neutron scattering (SANS) with contrast matching. Conformational-ensembles derived from SANS data indicated an increase in the overall size of FG Nups is associated with TF interaction. Moreover, the organization of the FG motif in the interacting state is consistent with prior experimental analyses defining that FG motifs undergo conformational restriction upon interacting with TFs. These results provide structural insights into a highly dynamic interaction and illustrate how functional disorder imparts rapid and selective FG Nup-TF interactions. Sparks et al. use small-angle neutron scattering experiments to describe the fuzzy interactions between disordered FG Nups and transport factors (TFs) from the nuclear pore complex, thus elucidating the subtle conformational changes that TFs induce within FG Nup chains. The study helps to define "fuzziness" at intermediate length scales.
KW - Contrast matching
KW - Ensemble analysis
KW - FG nucleoporins
KW - Intrinsically disordered proteins
KW - Kap95
KW - NTF2
KW - Nuclear pore complex
KW - Nuclear transport
KW - Small-angle neutron scattering
KW - Transport factors
UR - http://www.scopus.com/inward/record.url?scp=85041695788&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85041695788&partnerID=8YFLogxK
U2 - 10.1016/j.str.2018.01.010
DO - 10.1016/j.str.2018.01.010
M3 - Article
C2 - 29429880
AN - SCOPUS:85041695788
JO - Structure with Folding & design
JF - Structure with Folding & design
SN - 0969-2126
ER -