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.
|Number of pages||9|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - 2012|