Purification and photoaffinity labeling of fusicoccin receptors from maize

Aducci, Patrizia; Ballio, A.; Fogliano, Vincenzo; Fullone, Maria Rosaria; Marra, Mauro; Proietti, Noemi

doi:10.1111/j.1432-1033.1993.tb17929.x

Cited by 21 publications

(11 citation statements)

References 24 publications

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“…SDS-PAGE of the purified receptor showed two polypeptides with relative molecular masses of 30.5 kDa and 31.5 kDa, in agreement with earlier reports [3,4,6,8]. The 90 kDa polypeptide, assumed by one group [19] to be associated with the FCBP, could not be detected.…”

Section: Resultssupporting

confidence: 79%

The fusicoccin receptor of plants is a member of the 14‐3‐3 superfamily of eukaryotic regulatory proteins

1994

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The receptor for the wilt-inducing phytotoxin fusicoccin was purified to homogeneity from plasma membranes of Commelina communis as a complex with the radioligand [3H]9'-nor-8'-hydroxyfusicoccin. The preparation consisted of two polypeptides with apparent molecular masses of 30.5 kDa and 31.5 kDa and with isoelectric points of around pH 5.2 and 5.3, respectively. The proteins were N-terminally blocked. Internal amino acid sequences were obtained for both polypeptides of the fusicoccin-binding complex. Sequence information, as well as subsequent immunological analysis, proved that both polypeptides are members of the eukaryotic 143-3 family, which comprises structurally conserved regulatory proteins of widespread occurrence and a wide range of functions. 143-3 isoform(s) constituting the fusicoccin receptor are distinguishable from other cellular 143-3 proteins by their tight association with the plasma membrane. Applying temperature-induced Triton X-l 14 phase separation experiments, they, as well as the target enzyme of fusicoccin action, the H'-ATPase, partitioned into the phospholipid-rich fraction which contains the most hydrophobic proteins. The results discussed herein provide a basis for the elucidation of the molecular mechanism of fusicoccin action.

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Section: Resultssupporting

confidence: 79%

The fusicoccin receptor of plants is a member of the 14‐3‐3 superfamily of eukaryotic regulatory proteins

1994

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“…The FCBP was characterized in PM , * Corresponding author; e-mail fimca@imiucca.csi.unimi.it; fax 39 -2-26604399. from various plant tissues (Aducci and Ballio, 1989;Weiler et al, 1990) and highly purified FCBP preparations have been obtained (de Boer et al, 1989;Oecking and Weiler, 1991;Aducci et al, 1993;.…”

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confidence: 99%

Fusicoccin Binding to Its Plasma Membrane Receptor and the Activation of the Plasma Membrane H+-ATPase (III. Is There a Direct Interaction between the Fusicoccin Receptor and the Plasma Membrane H+-ATPase?)

et al. 1996

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“…were obtained as described previously (17). Briefly, crude solubilized receptors were prepared from maize shoot microsomes according to the method described by Aducci et al (18).…”

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confidence: 99%

Fusicoccin Effect on the in Vitro Interaction between Plant 14-3-3 Proteins and Plasma Membrane H+-ATPase

Fullone¹,

Visconti²,

Marra³

et al. 1998

Journal of Biological Chemistry

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A 17-amino acid peptide was selectively cleaved from the highly variant C terminus of the 33-kDa 14-3-3 isoform occurring in fusicoccin receptor preparations from maize and was sequenced. The determined C-terminal sequence was identical to that of the already known maize 14-3-3 homolog GF14-6, thus prompting the use of recombinant GF14-6 in an in vitro protein-protein interaction study. The cDNA of GF14-6 was expressed in Escherichia coli as a 32 P-phosphorylatable glutathione S-transferase fusion protein and was used as a probe in overlay experiments with H ؉ -ATPase partially purified from maize roots. The results demonstrated that the recombinant protein specifically bound to H ؉ -ATPase. The binding was dependent on Mg 2؉ and was strongly increased by fusicoccin. Controlled trypsin digestion of H ؉ -ATPase abolished the association with GF14-6, a finding that was suggestive of an interaction with the C terminus of the enzyme. To confirm this result, the Cterminal domain of H ؉ -ATPase was expressed as a glutathione S-transferase fusion peptide and was used in overlay experiments. GF14-6 was also able to bind to the isolated C terminus, but only in the presence of fusicoccin.

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Purification and photoaffinity labeling of fusicoccin receptors from maize

Cited by 21 publications

References 24 publications

The fusicoccin receptor of plants is a member of the 14‐3‐3 superfamily of eukaryotic regulatory proteins

The fusicoccin receptor of plants is a member of the 14‐3‐3 superfamily of eukaryotic regulatory proteins

Fusicoccin Binding to Its Plasma Membrane Receptor and the Activation of the Plasma Membrane H+-ATPase (III. Is There a Direct Interaction between the Fusicoccin Receptor and the Plasma Membrane H+-ATPase?)

Fusicoccin Effect on the in Vitro Interaction between Plant 14-3-3 Proteins and Plasma Membrane H+-ATPase

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