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.
journal_name
Proc Natl Acad Sci U S Aauthors
Venis MA,Napier RM,Barbier-Brygoo H,Maurel C,Perrot-Rechenmann C,Guern Jdoi
10.1073/pnas.89.15.7208keywords:
subject
Has Abstractpub_date
1992-08-01 00:00:00pages
7208-12issue
15eissn
0027-8424issn
1091-6490journal_volume
89pub_type
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更新日期:1999-10-12 00:00:00