Boutemy, Laurence S., King, Stuart R. F., Win, Joe, Hughes, Richard K., Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Blumenschein, Tharin M. A. ORCID: https://orcid.org/0000-0002-4932-5178, Kamoun, Sophien ORCID: https://orcid.org/0000-0002-0290-0315 and Banfield, Mark J. (2011) Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity. Journal of Biological Chemistry, 286 (41). pp. 35834-35842. ISSN 0021-9258
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Abstract
Phytopathogens deliver effector proteins inside host plant cells to promote infection. These proteins can also be sensed by the plant immune system, leading to restriction of pathogen growth. Effector genes can display signatures of positive selection and rapid evolution, presumably a consequence of their co-evolutionary arms race with plants. The molecular mechanisms underlying how effectors evolve to gain new virulence functions and/or evade the plant immune system are poorly understood. Here, we report the crystal structures of the effector domains from two oomycete RXLR proteins, Phytophthora capsici AVR3a11 and Phytophthora infestans PexRD2. Despite sharing
Item Type: | Article |
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Faculty \ School: | Faculty of Science > The Sainsbury Laboratory Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemistry |
UEA Research Groups: | Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Energy Materials Laboratory |
Depositing User: | Users 2731 not found. |
Date Deposited: | 24 Jan 2012 15:17 |
Last Modified: | 17 Jan 2024 01:19 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/36454 |
DOI: | 10.1074/jbc.M111.262303 |
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