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
  • Statistics
  • Help & Advice
University of Warwick

The Library

  • Login

Molecular cloning of ATR5Emoy2 from hyaloperonospora arabidopsidis, an avirulence determinant that triggers RPP5-mediated defense in Arabidopsis

Tools
- Tools
+ Tools

Bailey, Kate, Çevik, Volkan, Holton, Nicholas, Byrne-Richardson, Jane, Sohn, Kee Hoon, Coates, Mary, Woods-Tör, Alison, Aksoy, H. Murat, Hughes, L. (Linda), Baxter, Laura, Jones, Jonathan D. G., Beynon, Jim, 1956-, Holub, E. B. and Tör, Mahmut. (2011) Molecular cloning of ATR5Emoy2 from hyaloperonospora arabidopsidis, an avirulence determinant that triggers RPP5-mediated defense in Arabidopsis. Molecular Plant-Microbe Interactions, Vol.24 (No.7). pp. 827-838. ISSN 0894-0282

Full text not available from this repository.
Official URL: http://dx.doi.org/10.1094/MPMI-12-10-0278

Abstract

RPP5 is the seminal example of a cytoplasmic NB-LRR receptor-like protein that confers downy mildew resistance in Arabidopsis thaliana. In this study, we describe the cloning and molecular characterization of the gene encoding ATR5(Emoy2), an avirulence protein from the downy mildew pathogen Hyaloperonospora arabidopsidis isolate Emoy2. ATR5(Emoy2) triggers defense response in host lines expressing the functional RPP5 allele from Landsberg erecta (Ler-0). ATR5(Emoy2) is embedded in a cluster with two additional ATR5-like (ATR5L) genes, most likely resulting from gene duplications. ATR5L proteins do not trigger RPP5-mediated resistance and the copy number of ATR5L genes varies among H. arabidopsidis isolates. ATR5(Emoy2) and ATR5L proteins contain a signal peptide, canonical EER motif, and an RGD motif. However, they lack the canonical translocation motif RXLR, which characterizes most oomycete effectors identified so far. The signal peptide and the N-terminal regions including the EER motif of ATR5(Emoy2) are not required to trigger an RPP5-dependent immune response. Bioinformatics screen of H. arabidopsidis Emoy2 genome revealed the presence of 173 open reading frames that potentially encode for secreted proteins similar to ATR5(Emoy2), in which they share some motifs such as EER but there is no canonical RXLR motif.

Item Type: Journal Article
Subjects: Q Science > QH Natural history > QH426 Genetics
Divisions: Faculty of Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Molecular cloning, Arabidopsis, Proteins
Journal or Publication Title: Molecular Plant-Microbe Interactions
Publisher: American Phytopathological Society
ISSN: 0894-0282
Date: 2011
Volume: Vol.24
Number: No.7
Page Range: pp. 827-838
Identification Number: 10.1094/MPMI-12-10-0278
Status: Peer Reviewed
Publication Status: Published
Funder: Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC)
Grant number: BB/D000750/1 (BBSRC)
URI: http://wrap.warwick.ac.uk/id/eprint/39967

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item View Item
twitter

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