Journal article
Avirulence Protein 3a (AVR3a) from the Potato Pathogen Phytophthora infestans Forms Homodimers through Its Predicted Translocation Region and Does Not Specifically Bind Phospholipids
Stephan Wawra, Mark Agacan, Justin A Boddey, Ian Davidson, Claire MM Gachon, Matteo Zanda, Severine Grouffaud, Stephen C Whisson, Paul RJ Birch, Andy J Porter, Pieter van West
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2012
Abstract
The mechanism of translocation of RxLR effectors from plant pathogenic oomycetes into the cytoplasm of their host is currently the object of intense research activity and debate. Here, we report the biochemical and thermodynamic characterization of the Phytophthora infestans effector AVR3a in vitro. We show that the amino acids surrounding the RxLR leader mediate homodimerization of the protein. Dimerization was considerably attenuated by a localized mutation within the RxLR motif that was previously described to prevent translocation of the protein into host. Importantly, we confirm that the reported phospholipid-binding properties of AVR3a are mediated by its C-terminal effector domain, no..
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Awarded by Biotechnology and Biological Sciences Research Council
Awarded by Natural Environment Research Council
Funding Acknowledgements
This work was supported by the Biotechnology and Biological Sciences Research Council (BBSRC; to S. W., P. R. J. B., A. J. P., and P. v. W.), the Natural Environmental Research Council (NERC; to S. W., C. M. M. G., and P. v. W.), the University of Aberdeen (to S. G., I. D., A. J. P., M. Z., and P. v. W.), the University of Dundee (to M. A. and P. R. J. B.), the Scottish Government Rural and Environmental Science Analytical Services Division (RESAS; to S. C. W.), and The Royal Society (to P. v. W.).