Interaction of cryptogein with its binding sites in tobacco plasma membrane studied using the piezoelectric biosensor
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
19374882
DOI
10.1016/j.ab.2009.04.012
PII: S0003-2697(09)00251-6
Knihovny.cz E-resources
- MeSH
- Algal Proteins analysis metabolism MeSH
- Biosensing Techniques methods MeSH
- Cell Membrane metabolism MeSH
- Fungal Proteins MeSH
- Membrane Proteins analysis metabolism MeSH
- Phytophthora metabolism MeSH
- Plant Proteins metabolism MeSH
- Nicotiana metabolism MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Algal Proteins MeSH
- cryptogein protein, Phytophthora cryptogea MeSH Browser
- Fungal Proteins MeSH
- Membrane Proteins MeSH
- Plant Proteins MeSH
Elicitins are low-molecular-weight proteins representing the elicitor family secreted by many species of the oomycete Phytophthora. Elicitins induce a hypersensitive reaction in tobacco, a process that is triggered by binding of elicitin to the high-affinity site on the plasma membrane. Specific interaction of cryptogein with the binding sites on tobacco plasma membranes was studied using the piezoelectric biosensor in real time in a flow-through mode. Cryptogeins (wild-type and mutant forms) were covalently immobilized on the sensing surface, and membrane vesicles containing receptors were in solution. Kinetic characterization of the interaction provided values of kinetic rate association (k(a))=5.74 . 10(6)M(1)s(-1) and kinetic rate dissociation (k(d))=6.8710(-4)s(-1) constants, respectively. The kinetic equilibrium dissociation constant was calculated as K(D)=12.0 nM. The piezoelectric biosensor appeared to be a convenient tool for studying interactions of receptors embedded in membrane vesicles.
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