Antibodies to a peptide from the maize auxin-binding protein have auxin agonist activity
The major auxin-binding protein in maize membranes is thought to function as a physiological receptor. From earlier information, including the use of site-directed irreversible inhibitors, several of the amino acids likely to form part of the active auxin-binding site were provisionally assigned. In...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1992-08, Vol.89 (15), p.7208-7212 |
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Sprache: | eng |
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Zusammenfassung: | The major auxin-binding protein in maize membranes is thought to function as a physiological receptor. From earlier information, including the use of site-directed irreversible inhibitors, several of the amino acids likely to form part of the active auxin-binding site were provisionally assigned. Inspection of the amino acid sequence of the auxin-binding protein showed a short region containing all but one of these amino acids. We find that antisera raised against a synthetic peptide encompassing this region recognize all isoforms of the maize auxin-binding protein together with homologous polypeptides in other species. We further find that the antibodies hyperpolarize protoplast transmembrane potential in an auxin-like manner. We conclude that these antibodies display auxin agonist activity and that we have identified an essential portion of the auxin-binding site. |
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ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.89.15.7208 |