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 M.M. Gachon, Matteo Zanda, Severine Grouffaud, Stephen C. Whisson, Paul R.J. Birch, A.J. Porter, Pieter Van West

    Research output: Contribution to journalArticlepeer-review

    24 Citations (Scopus)

    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.
    Original languageEnglish
    Pages (from-to)38101-38109
    Number of pages9
    JournalJournal of Biological Chemistry
    Volume287
    Issue number45
    DOIs
    Publication statusPublished - 2012

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