Photoaffinity labeling of an herbicide receptor protein in chloroplast membranes
| Autor: | Gary Gardner, Katherine E. Steinback, Charles J. Arntzen, Klaus Pfister |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Multidisciplinary
Photoaffinity labeling Photosystem II Amaranthus hybridus food and beverages Biology biology.organism_classification Chloroplast chemistry.chemical_compound Membrane Biochemistry chemistry Biological Sciences: Botany Thylakoid heterocyclic compounds Sodium dodecyl sulfate Polyacrylamide gel electrophoresis |
| Zdroj: | Proceedings of the National Academy of Sciences. 78:981-985 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.78.2.981 |
| Popis: | 2-Azido-4-ethylamino-6-isopropylamino- s -triazine (azido-atrazine) inhibits photosynthetic electron transport at a site identical to that affected by atrazine (2-chloro-4-ethylamino-6-isopropylamino- s -triazine). The latter is a well-characterized inhibitor of photosystem II reactions. Azido-atrazine was used as a photoaffinity label to identify the herbicide receptor protein; UV irradiation of chloroplast thylakoids in the presence of azido[ 14 C]atrazine resulted in the covalent attachment of radioactive inhibitor to thylakoid membranes isolated from pea seedlings and from a triazine-susceptible biotype of the weed Amaranthus hybridus . No covalent binding of azido-atrazine was observed for thylakoid membranes isolated from a naturally occurring triazine-resistant biotype of A. hybridus . Analysis of thylakoid polypeptides from both the susceptible and resistant A. hybridus biotypes by sodium dodecyl sulfate/polyacrylamide gel electrophoresis, followed by fluorography to locate 14 C label, demonstrated specific association of the azido[ 14 C]atrazine with polypeptides of the 34- to 32-kilodalton size class in susceptible but not in resistant membranes. |
| Databáze: | OpenAIRE |
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