Structural basis of interaction of bipartite nuclear localization signal from Agrobacterium VirD2 with rice importin-alpha

Chang, Chiung-Wen, Williams, Simon J., Couñago, Rafael Miguez and Kobe, Bostjan (2014) Structural basis of interaction of bipartite nuclear localization signal from Agrobacterium VirD2 with rice importin-alpha. Molecular Plant, Advance Access 6: 1-10. doi:10.1093/mp/ssu014

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Author Chang, Chiung-Wen
Williams, Simon J.
Couñago, Rafael Miguez
Kobe, Bostjan
Title Structural basis of interaction of bipartite nuclear localization signal from Agrobacterium VirD2 with rice importin-alpha
Formatted title
Structural basis of interaction of bipartite nuclear localization signal from Agrobacterium VirD2 with rice importin-α
Journal name Molecular Plant   Check publisher's open access policy
ISSN 1674-2052
1752-9867
Publication date 2014-02-06
Year available 2014
Sub-type Article (original research)
DOI 10.1093/mp/ssu014
Volume Advance Access
Issue 6
Start page 1
End page 10
Total pages 10
Place of publication Oxford, United Kingdom
Publisher Oxford University Press
Collection year 2015
Language eng
Formatted abstract
...In conclusion, the aims of this study were to characterize the binding of bipartite NLSs to plant Impα, through investigating the binding of bipartite NLSs from VirD2, VirE2, and Npl to rImpα1aΔIBB. The affinities of VirE2-1 and VirE2-2 NLSs binding to rImpα1aΔIBB were found to be weak, likely due to these sequences being inconsistent with classical bipartite NLSs. We propose that neither NLS would facilitate efficient nuclear import, and that it is more likely that the NLS(s) are located in a different part of the protein, or that an adaptor protein facilitates the indirect recognition between VirE2 and Impα and consequently the nuclear import of VirE2 (Gelvin, 2010). We determined the first crystal structures of a plant Impα in complex with bipartite NLSs, those from VirD2 and Npl. The structures show that the binding of bipartite NLSs to plant, yeast and mouse Impα proteins is conserved; however, differences are found at the edges of the minor and major NLS-binding sites. Jointly, our study advances the general understanding of binding determinants of bipartite NLSs for Impα, and sheds light on the molecular basis of the import of Agrobacterial T-DNA to the plant cell nucleus.
Keyword Importin-α
Nuclear localization signal (NLS)
Nucleo-cytoplasmic transport
Agrobacterium-mediated transformation
Importin-alpha
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes First published online: February 6, 2014

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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Created: Fri, 14 Feb 2014, 10:44:53 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences