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Güttler, T.* ; Madl, T. ; Neumann, P.* ; Deichsel, D.* ; Corsini, L. ; Monecke, T.* ; Ficner, R.* ; Sattler, M. ; Görlich, D.*

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)
Verlagsversion DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter 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 Band: 17, Heft: 11, Seiten: 1367-1376 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Verlagsort New York, NY
Begutachtungsstatus Peer reviewed