The Library
Molecular cloning of ATR5Emoy2 from hyaloperonospora arabidopsidis, an avirulence determinant that triggers RPP5-mediated defense in Arabidopsis
Tools
Bailey, Kate, Cevik, Volkan, Holton, Nicholas, Byrne-Richardson, Jane, Sohn, Kee-Hoon, Coates, Mary, Woods-Tör, Alison, Aksoy, H. Murat, Hughes, L., Baxter, Laura, Jones, Jonathan D. G., Beynon, Jim, 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. doi:10.1094/MPMI-12-10-0278 ISSN 0894-0282.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
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, Engineering and Medicine > 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 | ||||
Official Date: | 2011 | ||||
Dates: |
|
||||
Volume: | Vol.24 | ||||
Number: | No.7 | ||||
Page Range: | pp. 827-838 | ||||
DOI: | 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) |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |