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Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector
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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 ISSN 0960-7412.
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Official URL: http://dx.doi.org/10.1111/tpj.12691
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 | ||||||||||
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Subjects: | Q Science > QH Natural history | ||||||||||
Divisions: | Faculty of Science, Engineering and Medicine > 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: |
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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 (Creative Commons) | ||||||||||
Date of first compliant deposit: | 28 December 2015 | ||||||||||
Date of first compliant Open Access: | 28 December 2015 | ||||||||||
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) |
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