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Nuclear import factors importin α and importin β undergo mutually induced conformational changes upon association
Author(s) -
Cingolani Gino,
Lashuel Hilal A.,
Gerace Larry,
Müller Christoph W.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02154-2
Subject(s) - importin , nuclear transport , nls , nuclear localization sequence , biophysics , chemistry , domain (mathematical analysis) , microbiology and biotechnology , biology , cell nucleus , nucleus , mathematics , mathematical analysis
A heterodimer of importin α and importin β accomplishes the nuclear import of proteins carrying classical nuclear localization signals (NLS). The interaction between the two import factors is mediated by the IBB domain of importin α and involves an extended recognition surface as shown by X‐ray crystallography. Using a combination of biochemical and biophysical techniques we have investigated the formation of the importin β:IBB domain complex in solution. Our data suggest that upon binding to the IBB domain, importin β adopts a compact, proteolytically resistant conformation, while simultaneously the IBB domain folds into an α helix. We suggest a model to describe how these dual mutually induced conformational changes may orchestrate the nuclear import of NLS cargo in vivo.