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
Hauptverfasser: Venis, M.A. (Horticulture Research International, East Malling, Kent, UK), Napier, R.M, Barbier-Brygoo, H, Maurel, C, Perrot-Rechenmann, C, Guern, J
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container_issue 15
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container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 89
creator Venis, M.A. (Horticulture Research International, East Malling, Kent, UK)
Napier, R.M
Barbier-Brygoo, H
Maurel, C
Perrot-Rechenmann, C
Guern, J
description 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.
doi_str_mv 10.1073/pnas.89.15.7208
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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. 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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. 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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.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>1323130</pmid><doi>10.1073/pnas.89.15.7208</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0002-4255-6440</orcidid><oa>free_for_read</oa></addata></record>
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ispartof Proceedings of the National Academy of Sciences - PNAS, 1992-08, Vol.89 (15), p.7208-7212
issn 0027-8424
1091-6490
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subjects activity
Agonists
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Antibodies
ANTICORPS
ANTICUERPOS
Antiserum
auxin-binding protein
AUXINAS
AUXINE
Auxins
Biological and medical sciences
Cell membranes
Cellular Biology
Corn
Fundamental and applied biological sciences. Psychology
Indoleacetic Acids - metabolism
Intracellular Membranes - drug effects
Intracellular Membranes - physiology
Life Sciences
LIGAND
LIGANDOS
MEMBRANA
MEMBRANE
membrane potential
Membrane Proteins - isolation & purification
Membranes
Microsomes - drug effects
Microsomes - physiology
Molecular Sequence Data
Molecular Weight
Naphthaleneacetic Acids - pharmacology
Other biological molecules
PEPTIDE
Peptides - chemical synthesis
Peptides - immunology
PEPTIDOS
Plant Growth Regulators
Plant growth substances
Plant Physiological Phenomena
Plant Proteins
Protein isoforms
PROTEINAS
PROTEINE
Proteins
Protoplasts
Protoplasts - physiology
Receptors
Receptors, Cell Surface - immunology
Receptors, Cell Surface - isolation & purification
Receptors, Cell Surface - metabolism
Space life sciences
ZEA MAYS
Zea mays - physiology
title Antibodies to a peptide from the maize auxin-binding protein have auxin agonist activity
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