Transgenic expression of the von Willebrand a domain of the BONZAI1/COPINE 1 protein triggers a lesion-mimic phenotype in Arabidopsis

Jianxin Liu, Niranjani Jambunathan, Timothy W. McNellis

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


The copines are a newly identified, widely distributed class of Ca 2+-dependent, phospholipid-binding proteins that may be involved in cellular signaling. The copines have a characteristic domain structure: two C2 domains in the N-terminal region and a von Willebrand A (VWA) domain in the C-terminal region. Studies suggest that copines interact with target protein(s) via their VWA domain and recruit the proteins to a membrane location through the activity of the C2 domains. Arabidopsis thaliana (L.) Heynh. plants with loss-of-function mutations in the BONZAI 1/COPINE 1 (BON1/CPN1) gene display aberrant regulation of defense responses, including development of a lesion-mimic phenotype, an accelerated hypersensitive response, and increased resistance to a bacterial and an oomycetous pathogen. The phenotype of mutants in BON1/CPN1 is both humidity- and temperature-sensitive. In this study, we generated transgenic plants expressing either the VWA or the C2 portions of BON1/CPN1 in the wild-type Columbia-0 (Col-0) genetic background. Transgenic plants expressing the BON1/CPN1 C2 domain portion appeared like wild-type plants. However, transgenic plants expressing the BON1/CPN1 VWA domain exhibited a lesion-mimic phenotype that partially phenocopied bon1/cpn1 mutant plants. Our data suggest that BON1/CPN1 VWA domain fragments may interfere with the function of the full-length endogenous BON1/CPN1 protein, possibly by competing with the full-length BON1/CPN1 protein for association with target proteins normally bound to the full-length BON1/CPN1 protein.

Original languageEnglish (US)
Pages (from-to)85-94
Number of pages10
Issue number1
StatePublished - Apr 2005

All Science Journal Classification (ASJC) codes

  • Genetics
  • Plant Science


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