Utilizing the Dyn2 dimerization-zipper as a tool to probe NPC structure and function.
Methods Cell Biol
; 122: 99-115, 2014.
Article
em En
| MEDLINE
| ID: mdl-24857727
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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MEDLINE
Assunto principal:
Saccharomyces cerevisiae
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Dineínas
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Poro Nuclear
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Complexo de Proteínas Formadoras de Poros Nucleares
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Proteínas de Saccharomyces cerevisiae
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article