1994
DOI: 10.1073/pnas.91.2.689
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Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by 5-azido-[7-3H]indole-3-acetic acid: identification of a glutathione S-transferase.

Abstract: We used 5-azido-[7-3Hjindole-3-acetic acid (5-azido-[7-3H]IAA), a photoaffinity analogue of the plant hormone indole-3-acetic acid (IAA), to search for auxinbinding proteins in Arabidopsis thaliana membranes. We identified an auxin-binding protein with a molecular mass of 24 kDa (Atpm24) in microsomes as well as in plasma membrane vesicles. Atpm24 was solubilized by 1% Triton X-100 and partially purified. A cDNA clone (Atpm24.1) corresponding to Atpm24 was isolated. The amino acid sequence predicted from the A… Show more

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Cited by 132 publications
(78 citation statements)
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“…In tobacco cell cultures, glutathione S-transferase mRNA accumulated in response to auxin treatment (Takahashi and Nagata, 1992;Droog et al, 1993). Furthermore, the binding of indole-3-acetic acid to glutathione S-transferases from Hyoscyumus muticus (Bilang et al, 1993) and Arubidopsis thaliunu (Zettl et al, 1994) has been demonstrated by photoaffinity labeling with a tritiated indole-3-acetic acid analog, suggesting that at least some glutathione S-transferases are either regulated by this phytohormone or are involved in its metabolism. Recently, two reports provided evidence for a correlation of plant glutathione S-transferases with pathogen defence : firstly, glutathione S-transferase ac-tivity has been shown to be induced by fungal elicitor in cultured french bean cells (Edwards and Dixon, 1991), and, secondly, one member of the wheat glutathione S-transferase family is specifically activated by pathogen attack or glutathione, but not by xenobiotics (Mauch and Dudler, 1993).…”
mentioning
confidence: 95%
“…In tobacco cell cultures, glutathione S-transferase mRNA accumulated in response to auxin treatment (Takahashi and Nagata, 1992;Droog et al, 1993). Furthermore, the binding of indole-3-acetic acid to glutathione S-transferases from Hyoscyumus muticus (Bilang et al, 1993) and Arubidopsis thaliunu (Zettl et al, 1994) has been demonstrated by photoaffinity labeling with a tritiated indole-3-acetic acid analog, suggesting that at least some glutathione S-transferases are either regulated by this phytohormone or are involved in its metabolism. Recently, two reports provided evidence for a correlation of plant glutathione S-transferases with pathogen defence : firstly, glutathione S-transferase ac-tivity has been shown to be induced by fungal elicitor in cultured french bean cells (Edwards and Dixon, 1991), and, secondly, one member of the wheat glutathione S-transferase family is specifically activated by pathogen attack or glutathione, but not by xenobiotics (Mauch and Dudler, 1993).…”
mentioning
confidence: 95%
“…In addition, it seems likely that GSTs may also function as a reversible ligand (Zettl et al, 1994) and it is with this function that they may play a role in hormonal regulation. The Arabidopsis GST Atpm24.1 was shown to bind to the photoaffinity analog of indole-3-acetic acid.…”
mentioning
confidence: 99%
“…The large family of GSTs (Table 1) were the first auxin-inducible genes associated with enzymic activity (Takahashi & Nagata, 1992 a). These proteins are also of interest because they have been shown to bind the photoactive auxin derivative azido-IAA (Bilang et al, 1993 ;Zettl, Schell & Palme, 1994). Even so, the role of GSTs in auxin action remains unresolved.…”
Section: Functions Of Auxin-inducible Proteins and Auxin Bindingmentioning
confidence: 99%
“…Apart from transport proteins azido-IAA has been found to label a number of other polypeptides, a superoxide dismutase (Feldwisch et al, 1994), a /?-1,3-glucanase (Macdonald, Jones & King, 1991), GSTs-both soluble (Bilang et al, 1993) and membrane-bound (Zettl et al, 1994) -and a 60 kDa protein having /?-glucosidase activity . We have already discussed GSTs and the possible significance of their role in auxin action [Section II.7(a)].…”
Section: Other Auxin Binding Proteinsmentioning
confidence: 99%
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