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Open Access Green as soon as Postprint is submitted to ZB.
NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1.
Nat. Struct. Mol. Biol. 17, 1367-1376 (2010)
Classic nuclear export signals (NESs) confer CRM1-dependent nuclear export. Here we present crystal structures of the RanGTP-CRM1 complex alone and bound to the prototypic PKI or HIV-1 Rev NESs. These NESs differ markedly in the spacing of their key hydrophobic (Φ) residues, yet CRM1 recognizes them with the same rigid set of five Φ pockets. The different Φ spacings are compensated for by different conformations of the bound NESs: in the case of PKI, an α-helical conformation, and in the case of Rev, an extended conformation with a critical proline docking into a Φ pocket. NMR analyses of CRM1-bound and CRM1-free PKI NES suggest that CRM1 selects NES conformers that pre-exist in solution. Our data lead to a new structure-based NES consensus, and explain why NESs differ in their affinities for CRM1 and why supraphysiological NESs bind the exportin so tightly.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Cross-correlated relaxation; order chromosome structure; automated noe assignment; NMR-spectroscopy; Leptomycin-B; HIV-1 REV; Ribosomal-subunits; Protein structures; Activation domain; Tansfer-RNA
ISSN (print) / ISBN
1545-9993
e-ISSN
1545-9985
Quellenangaben
Volume: 17,
Issue: 11,
Pages: 1367-1376
Publisher
Nature Publishing Group
Publishing Place
New York, NY
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)