Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-α

Fontes, R. Marcos, Teh, Trazel, Jans, David A., Brinkworth, Ross I. and Kobe, Bostjan (2003) Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-α. Journal of Biological Chemistry, 278 30: 27981-27987. doi:10.1074/jbc.M303275200

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Author Fontes, R. Marcos
Teh, Trazel
Jans, David A.
Brinkworth, Ross I.
Kobe, Bostjan
Title Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-α
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2003-01-01
Sub-type Article (original research)
DOI 10.1074/jbc.M303275200
Open Access Status File (Publisher version)
Volume 278
Issue 30
Start page 27981
End page 27987
Total pages 7
Editor Herbert Tabor
Place of publication Bethesda
Publisher American Society for Biochemistry and Molecular Biology, Inc.
Collection year 2003
Language eng
Subject C1
270103 Protein Targeting and Signal Transduction
780105 Biological sciences
Abstract Importin-alpha is the nuclear import receptor that recognizes cargo proteins carrying conventional basic monopartite and bipartite nuclear localization sequences (NLSs) and facilitates their transport into the nucleus. Bipartite NLSs contain two clusters of basic residues, connected by linkers of variable lengths. To determine the structural basis of the recognition of diverse bipartite NLSs by mammalian importin-alpha, we co-crystallized a non-autoinhibited mouse receptor protein with peptides corresponding to the NLSs from human retinoblastoma protein and Xenopus laevis phosphoprotein N1N2, containing diverse sequences and lengths of the linker. We show that the basic clusters interact analogously in both NLSs, but the linker sequences adopt different conformations, whereas both make specific contacts with the receptor. The available data allow us to draw general conclusions about the specificity of NLS binding by importin-alpha and facilitate an improved definition of the consensus sequence of a conventional basic/bipartite NLS (KRX10-12KRRK) that can be used to identify novel nuclear proteins.
Keyword T-antigen Nls
Protein-kinase
Karyopherin-alpha
Crystallographic Analysis
Substrate-specificity
Enhances Recognition
In-vivo
Signal
Site
Transport
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 12:09:38 EST