Similarity, in molecular structure and function, between the plant toxin purothionin and the mammalian pore-forming proteins

T. Oka, Y. Murata, T. Nakanishi, H. Yoshizumi, H. Hayashida, Y. Ohtsuki, K. Toyoshima, A. Hakura

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23 Citations (Scopus)

Abstract

Many proteins containing domains of a cysteine-rich repeated motif, such as epidermal growth factor (EGF), have been reported. Here we report strong similarity between the amino acid sequence of a plant toxin-i.e., purothionin and its homologues-and with those of a domain found in mammalian pore-forming cytoplasmic proteins: components of complement and perforin of cytotoxic T- lymphocytes or natural killer-like cytotoxic cells. These similar sequences were found to be identical to the so-called EGF-like cysteine-rich repeated motif itself. Electronmicroscopic observations indicated that, like complement and perforin, purothionin forms pores in the cytoplasmic membrane of target cells, resulting in their death within a few hours. On the basis of these sequence comparisons and physiological functions, we propose a scheme for the evolution of proteins containing modules of the cysteine-rich repeat motif.

Original languageEnglish
Pages (from-to)707-715
Number of pages9
JournalMolecular Biology and Evolution
Volume9
Issue number4
Publication statusPublished - Jan 1 1992

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Keywords

  • cystein-rich repeat motif
  • perforin
  • phylogeny
  • pore-forming proteins (PFP)
  • purothionin

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Molecular Biology
  • Genetics

Cite this

Oka, T., Murata, Y., Nakanishi, T., Yoshizumi, H., Hayashida, H., Ohtsuki, Y., Toyoshima, K., & Hakura, A. (1992). Similarity, in molecular structure and function, between the plant toxin purothionin and the mammalian pore-forming proteins. Molecular Biology and Evolution, 9(4), 707-715.