Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats

Richard Bayliss, Sara W. Leung, Rosanna P. Baker, B. Booth Quimby, Anita H. Corbett, Murray Stewart

Research output: Contribution to journalArticlepeer-review

Abstract

Interactions with nucleoporins containing FxFG-repeat cores are crucial for the nuclear import of RanGDP mediated by nuclear transport factor 2 (NTF2). We describe here the 1.9 Å resolution crystal structure of yeast NTF2-N77Y bound to a FxFG-nucleoporin core, which provides a basis for understanding this interaction and its role in nuclear trafficking. The two identical FxFG binding sites on the dimeric molecule are formed by residues from each chain of NTF2. Engineered mutants at the interaction interface reduce the binding of NTF2 to nuclear pores and cause reduced growth rates and Ran mislocalization when substituted for the wild-type protein in yeast. Comparison with the crystal structure of FG-nucleoporin cores bound to importin-β and TAP/pl5 identified a number of common features of their binding sites. The structure of the binding interfaces on these transport factors provides a rationale for the specificity of their interactions with nucleoporins that, combined with their weak binding constants, facilitates rapid translocation through NPCs during nuclear trafficking.

Original languageEnglish (US)
Pages (from-to)2843-2853
Number of pages11
JournalEMBO Journal
Volume21
Issue number12
DOIs
StatePublished - Jun 17 2002
Externally publishedYes

Keywords

  • FxFG repeats
  • NTF2
  • Nuclear trafficking

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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