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

Ho Yee Joyce Fung, Szu Chin Fu, Chad A Brautigam, Yuh Min Chook

Research output: Contribution to journalArticle

26 Citations (Scopus)

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.

Original languageEnglish (US)
Article numbere10034
JournaleLife
Volume4
Issue numberSeptember 2015
DOIs
StatePublished - Sep 8 2015

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Nuclear Export Signals
Karyopherins
Chromosomes
Maintenance
Protein Sorting Signals
Proteome
Plasticity
Crystal structure
Chromosome Structures
Cell Nucleus Active Transport
Proteins

ASJC Scopus subject areas

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

Cite this

Structural determinants of nuclear export signal orientation in binding to exportin CRM1. / Fung, Ho Yee Joyce; Fu, Szu Chin; Brautigam, Chad A; Chook, Yuh Min.

In: eLife, Vol. 4, No. September 2015, e10034, 08.09.2015.

Research output: Contribution to journalArticle

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