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

Takashi Oka, Yoshiaki Murata, Toshihiro Nakanishi, Hajime Yoshizumi, Hidenori Hayashida, Yuji Ohtsuki, Kumao Toyoshima, Akira Hakura

Research output: Contribution to journalArticle

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 perform 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 perform, 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 - 1992
Externally publishedYes

Fingerprint

Porins
phytotoxins
Molecular Structure
chemical structure
Molecular structure
toxin
Cysteine
cysteine
epidermal growth factor
Epidermal Growth Factor
protein
complement
Proteins
cytotoxic T-lymphocytes
T-cells
proteins
Cytotoxic T-Lymphocytes
cell membranes
Amino Acid Sequence
Complement System Proteins

Keywords

  • Cystein-rich repeat motif
  • Perforin
  • Phylogeny
  • Pore-forming proteins (PFP)
  • Purothionin

ASJC Scopus subject areas

  • Genetics
  • Biochemistry
  • Genetics(clinical)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Ecology, Evolution, Behavior and Systematics
  • Agricultural and Biological Sciences (miscellaneous)
  • Molecular Biology

Cite this

Oka, T., Murata, Y., Nakanishi, T., Yoshizumi, H., Hayashida, H., Ohtsuki, Y., ... 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.

Similarity, in molecular structure and function, between the plant toxin purothionin and the mammalian pore-forming proteins. / Oka, Takashi; Murata, Yoshiaki; Nakanishi, Toshihiro; Yoshizumi, Hajime; Hayashida, Hidenori; Ohtsuki, Yuji; Toyoshima, Kumao; Hakura, Akira.

In: Molecular Biology and Evolution, Vol. 9, No. 4, 1992, p. 707-715.

Research output: Contribution to journalArticle

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, vol. 9, no. 4, pp. 707-715.
Oka, Takashi ; Murata, Yoshiaki ; Nakanishi, Toshihiro ; Yoshizumi, Hajime ; Hayashida, Hidenori ; Ohtsuki, Yuji ; Toyoshima, Kumao ; Hakura, Akira. / Similarity, in molecular structure and function, between the plant toxin purothionin and the mammalian pore-forming proteins. In: Molecular Biology and Evolution. 1992 ; Vol. 9, No. 4. pp. 707-715.
@article{7813faaa39ee44a5aa20715b80ac38ea,
title = "Similarity, in molecular structure and function, between the plant toxin purothionin and the mammalian pore-forming proteins",
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 perform 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 perform, 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.",
keywords = "Cystein-rich repeat motif, Perforin, Phylogeny, Pore-forming proteins (PFP), Purothionin",
author = "Takashi Oka and Yoshiaki Murata and Toshihiro Nakanishi and Hajime Yoshizumi and Hidenori Hayashida and Yuji Ohtsuki and Kumao Toyoshima and Akira Hakura",
year = "1992",
language = "English",
volume = "9",
pages = "707--715",
journal = "Molecular Biology and Evolution",
issn = "0737-4038",
publisher = "Oxford University Press",
number = "4",

}

TY - JOUR

T1 - Similarity, in molecular structure and function, between the plant toxin purothionin and the mammalian pore-forming proteins

AU - Oka, Takashi

AU - Murata, Yoshiaki

AU - Nakanishi, Toshihiro

AU - Yoshizumi, Hajime

AU - Hayashida, Hidenori

AU - Ohtsuki, Yuji

AU - Toyoshima, Kumao

AU - Hakura, Akira

PY - 1992

Y1 - 1992

N2 - 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 perform 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 perform, 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.

AB - 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 perform 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 perform, 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.

KW - Cystein-rich repeat motif

KW - Perforin

KW - Phylogeny

KW - Pore-forming proteins (PFP)

KW - Purothionin

UR - http://www.scopus.com/inward/record.url?scp=0026629363&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026629363&partnerID=8YFLogxK

M3 - Article

C2 - 1630308

AN - SCOPUS:0026629363

VL - 9

SP - 707

EP - 715

JO - Molecular Biology and Evolution

JF - Molecular Biology and Evolution

SN - 0737-4038

IS - 4

ER -