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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1992 Aug 1;89(15):7208–7212. doi: 10.1073/pnas.89.15.7208

Antibodies to a peptide from the maize auxin-binding protein have auxin agonist activity.

M A Venis 1, R M Napier 1, H Barbier-Brygoo 1, C Maurel 1, C Perrot-Rechenmann 1, J Guern 1
PMCID: PMC49675  PMID: 1323130

Abstract

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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Selected References

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