Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector

Tools
- Tools
+ Tools

Wirthmueller, Lennart, Roth, Charlotte, Fabro, Georgina, Caillaud, Marie-Cécile, Rallapalli, Ghanasyam, Asai, Shuta, Sklenar, Jan, Jones, Alexandra M., Wiermer, Marcel, Jones, Jonathan D. G. and Banfield, Mark J. (2015) Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector. The Plant Journal, Volume 81 (Number 1). pp. 40-52. doi:10.1111/tpj.12691

[img] PDF
WRAP_Jones_14Wirthmueller_PlantJ.pdf - Accepted Version
Embargoed item. Restricted access to Repository staff only - Requires a PDF viewer.

Download (621Kb)
[img]
Preview
PDF (Creative Commons : Attribution 4.0)
WRAP_Jones_tpj12691.pdf - Published Version - Requires a PDF viewer.

Download (1798Kb) | Preview
Official URL: http://dx.doi.org/10.1111/tpj.12691

Request Changes to record.

Abstract

Importin-αs are essential adapter proteins that recruit cytoplasmic proteins destined for active nuclear import to the nuclear transport machinery. Cargo proteins interact with the importin-α armadillo repeat domain via nuclear localization sequences (NLSs), short amino acids motifs enriched in Lys and Arg residues. Plant genomes typically encode several importin-α paralogs that can have both specific and partially redundant functions. Although some cargos are preferentially imported by a distinct importin-α, it remains unknown how this specificity is generated and to what extent cargos compete for binding to nuclear transport receptors. Here we report that the effector protein HaRxL106 from the oomycete pathogen Hyaloperonospora arabidopsidis co-opts the host cell's nuclear import machinery. We use HaRxL106 as a probe to determine redundant and specific functions of importin-α paralogs from Arabidopsis thaliana. A crystal structure of the importin-α3/MOS6 armadillo repeat domain suggests that five of the six Arabidopsis importin-αs expressed in rosette leaves have an almost identical NLS binding site. Comparison of the importin-α binding affinities of HaRxL106 and other cargos in vitro and in plant cells suggests that relatively small affinity differences in vitro affect the rate of transport complex formation in vivo. Our results suggest that cargo affinity for importin-α, sequence variation at the importin-α NLS binding sites and tissue-specific expression levels of importin-αs determine formation of cargo/importin-α transport complexes in plant cells.

Item Type: Journal Article
Subjects: Q Science > QH Natural history
Divisions: Faculty of Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Cytoplasm, Peronosporaceae, Arabidopsis thaliana, Plants -- Disease and pest resistance
Journal or Publication Title: The Plant Journal
Publisher: Wiley-Blackwell Publishing Ltd.
ISSN: 0960-7412
Official Date: January 2015
Dates:
DateEvent
January 2015Published
17 November 2014Available
29 September 2014Accepted
5 June 2014Submitted
Volume: Volume 81
Number: Number 1
Number of Pages: 13
Page Range: pp. 40-52
DOI: 10.1111/tpj.12691
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
Funder: Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Gatsby Charitable Foundation (GCF), John Innes Centre, Federation of European Biochemical Societies (FEBS), Deutsche Forschungsgemeinschaft (DFG), European Molecular Biology Organization (EMBO), Seventh Framework Programme (European Commission) (FP7)
Grant number: BBJ00453 (BBSRC), BBK009176 (BBSRC)

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us