Document Detail

Thionins: properties, possible biological roles and mechanisms of action.
MedLine Citation:
PMID:  7948874     Owner:  NLM     Status:  MEDLINE    
Thionins are low-molecular-weight proteins (M(r) ca. 5000) occurring in seeds, stems, roots and leaves of a number of plant species. The different members of this family of plant proteins show both sequence and structural homology, and are toxic to bacteria, fungi, yeasts and various naked cells in vitro. Toxicity requires an electrostatic interaction of the positively charged thionin with the negatively charged phospholipids making up the membrane, followed by either pore formation or a specific interaction with a certain lipid domain. This domain might be composed of phosphoinositides, which mediate transduction of environmental signals in eukaryotes. Their in vitro toxicity to plant pathogenic bacteria and fungi could reflect a direct role in plant defence, although, in view of the many divergent activities displayed by thionins both in vitro and in vivo, a biological role other than inhibition of microbial growth is equally plausible.
D E Florack; W J Stiekema
Related Documents :
10508754 - Protein farnesylation in plants: a greasy tale.
19220784 - Illuminated behaviour: phytochrome as a key regulator of light foraging and plant anti-...
9592124 - Short chain oligogalacturonides induce ethylene production and expression of the gene e...
16809044 - Diverse signals converge at mapk cascades in plant.
22122664 - The wavy growth 3 e3 ligase family controls the gravitropic response in arabidopsis roots.
25096754 - Apoplastic peroxidases are required for salicylic acid-mediated defense against pseudom...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Plant molecular biology     Volume:  26     ISSN:  0167-4412     ISO Abbreviation:  Plant Mol. Biol.     Publication Date:  1994 Oct 
Date Detail:
Created Date:  1994-12-16     Completed Date:  1994-12-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9106343     Medline TA:  Plant Mol Biol     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  25-37     Citation Subset:  IM    
DLO Centre for Plant Breeding and Reproduction Research (CPRO-DLO), Department of Molecular Biology, Wageningen, Netherlands.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Sequence
Models, Molecular
Molecular Sequence Data
Plant Proteins / chemistry,  genetics,  physiology*,  toxicity
Toxins, Biological / chemistry,  genetics,  metabolism*,  toxicity
Reg. No./Substance:
0/Plant Proteins; 0/Toxins, Biological

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Isolation of a pea (Pisum sativum) seed lipoxygenase promoter by inverse polymerase chain reaction a...
Next Document:  The major biotinyl protein from Pisum sativum seeds covalently binds biotin at a novel site.