Structural determinants of nuclear export signal orientation in binding to exportin CRM1

ELife
Ho Yee Joyce FungYuh Min Chook

Abstract

The Chromosome Region of Maintenance 1 (CRM1) protein mediates nuclear export of hundreds of proteins through recognition of their nuclear export signals (NESs), which are highly variable in sequence and structure. The plasticity of the CRM1-NES interaction is not well understood, as there are many NES sequences that seem incompatible with structures of the NES-bound CRM1 groove. Crystal structures of CRM1 bound to two different NESs with unusual sequences showed the NES peptides binding the CRM1 groove in the opposite orientation (minus) to that of previously studied NESs (plus). Comparison of minus and plus NESs identified structural and sequence determinants for NES orientation. The binding of NESs to CRM1 in both orientations results in a large expansion in NES consensus patterns and therefore a corresponding expansion of potential NESs in the proteome.

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Citations

Mar 2, 2016·Wiley Interdisciplinary Reviews. RNA·Jason D FernandesAlan D Frankel
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May 12, 2018·The Journal of Cell Biology·Metin AksuDirk Görlich
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Mar 16, 2021·Molecular Biology of the Cell·Ho Yee Joyce FungYuh Min Chook
Jun 26, 2020·Journal of Medicinal Chemistry·Alaa ShaikhqasemRalf Ficner
May 1, 2021·International Journal of Molecular Sciences·Baojin Ding, Masood Sepehrimanesh

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Methods Mentioned

BETA
pull-down
microscale thermophoresis
size-exclusion chromatography
gel filtration
nucleotide exchange
ion exchange chromatography
electrophoresis

Software Mentioned

phenix
PyMOL
3000
HKL
GUSSI
GraphPad Prism
PALMIST
ImageJ
Linux
Molprobity

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