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
S Wawra, M Agacan, JA Boddey, I Davidson, CMM Gachon, M Zanda, S Grouffaud, SC Whisson, PRJ Birch, AJ Porter, P Van West
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2012
Abstract
Background: AVR3a is a Phytophthora infestans effector that translocates into potato cells dependent on the N-terminal RxLR leader. Results: AVR3a dimerization is inhibited by a mutation that also impairs translocation. Conclusion: Phospholipid binding of AVR3a is probably physiologically irrelevant because only denatured protein molecules bind. Significance: Our findings will help us to understand how oomycete RxLR effectors function. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
Grants
Awarded by Biotechnology and Biological Sciences 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.).