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    2. College of Bioresources and Agriculture / 生物資源暨農學院
    3. Agricultural Chemistry / 農業化學系
    4. Nonhost resistance of tomato to the bean pathogen Pseudomonas syringae pv. syringae B728a is due to a defective E3 ubiquitin ligase domain in AvrPtoB B728a
     
    • Details

    Nonhost resistance of tomato to the bean pathogen Pseudomonas syringae pv. syringae B728a is due to a defective E3 ubiquitin ligase domain in AvrPtoB B728a

    Journal
    Molecular Plant-Microbe Interactions
    Journal Volume
    26
    Journal Volume
    26
    Journal Issue
    4
    Journal Issue
    4
    Pages
    387-397
    Start Page
    387
    End Page
    397
    ISSN
    08940282
    Date Issued
    2013-04
    Author(s)
    Chien, Ching-Fang
    Mathieu, Johannes
    CHUN-HUA HSU  
    Boyle, Patrick
    Martin, Gregory B.
    NAI-CHUN LIN  
    DOI
    10.1094/MPMI-08-12-0190-R
    URI
    https://scholars.lib.ntu.edu.tw/handle/123456789/446202
    https://www.scopus.com/pages/publications/84874630416?origin=resultslist
    URL
    https://www2.scopus.com/inward/record.uri?eid=2-s2.0-84874630416&doi=10.1094%2fMPMI-08-12-0190-R&partnerID=40&md5=2f86b5c39b52b7ddede76376ebaa6abb
    Abstract
    The bean pathogen Pseudomonas syringae pv. syringae B728a expresses homologs of the type III effectors AvrPto and AvrPtoB, either of which can trigger resistance in tomato cultivars expressing Pto and Prf genes. We found that strain B728a also elicits nonhost resistance in tomato cultivars VFNT Cherry and Moneymaker that lack Pto but express other members of the Pto family (e.g., SlFen and SlPtoC). Here, we show that the AvrPtoB homolog from B728a, termed AvrPtoBB728a (also known as HopAB1), is recognized by 'VFNT Cherry' and 'Moneymaker' when the effector is expressed in P. syringae pv. syringae 61, a strain lacking the avrPto or avrPtoB homolog. Using a gene-silencing approach, this recognition was shown to involve one or more Pto family members and Prf. AvrPtoBB728a interacted with SlFen, SlPtoC, and SlPtoD, in addition to Pto, in a yeast two-hybrid assay. In P. syringae pv. tomato DC3000, the C-terminal domain of AvrPtoB is an E3 ubiquitin ligase that ubiquitinates Fen, causing its degradation and leading to disease susceptibility. Although the C-terminal domain of AvrPtoBB728a shares 69% amino acid identity with that of AvrPtoB, we found that it has greatly reduced E3 ligase activity and is unable to ubiquitinate Fen in an in vitro ubiquitination assay. Thus, the nonhost resistance of 'VFNT Cherry' and 'Moneymaker' to B728a appears to be due to recognition of AvrPtoBB728 as a result of the effector's reduced E3 ligase activity, which prevents it from facilitating degradation of a Pto family member. We speculate that the primary plant host of B728a lacks a Fen-like protein and that, therefore, the E3 ligase of AvrPtoBB728 was unnecessary for pathogenicity and has diverged and become ineffective.
    Type
    journal article

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