Utilizing the Dyn2 dimerization-zipper as a tool to probe NPC structure and function
The discovery of dynein light chain 2 (Dyn2) as a member of the nucleoporins in yeast led to a series of applications to study NPC structure and function. Its intriguing ability to act as a hub for the parallel dimerization of two short amino acid sequence motifs (DID) prompted us to utilize it as a...
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| Hauptverfasser: | , , |
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| Dokumenttyp: | Kapitel/Artikel |
| Sprache: | Englisch |
| Veröffentlicht: |
20 May 2014
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| In: |
Nuclear pore complexes and nucleocytoplasmic transport
Year: 2014, Pages: 99-115 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/B9780124171602000059
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| Verfasserangaben: | Dirk Flemming, Philipp Stelter, and Ed Hurt |
MARC
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| 520 | |a The discovery of dynein light chain 2 (Dyn2) as a member of the nucleoporins in yeast led to a series of applications to study NPC structure and function. Its intriguing ability to act as a hub for the parallel dimerization of two short amino acid sequence motifs (DID) prompted us to utilize it as a tool for probing nucleocytoplasmic transport in vivo. Further, the distinct structure of the Dyn2-DID rod, which is easily visible in the electron microscope, allowed us to develop a precise structural label on proteins or protein complexes. This label was used to identify the position of subunits in NPC subcomplexes or to derive at pseudo-atomic models of single large Nups. The versatility for various applications of the DID-Dyn2 system makes it an attractive molecular tool beyond the nuclear pore and transport field. | ||
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| 650 | 4 | |a Dynein2 | |
| 650 | 4 | |a Electron microscopy | |
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| 650 | 4 | |a Negative stain | |
| 650 | 4 | |a NPC | |
| 650 | 4 | |a Transport channel | |
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