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The fusicoccin receptor of plants is a member of the 14‐3‐3 superfamily of eukaryotic regulatory proteins
Author(s) -
Oecking C.,
Eckerskorn C.,
Weiler E.W.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00949-x
Subject(s) - fusicoccin , biochemistry , biology , isoelectric point , receptor , gene isoform , peptide sequence , atpase , enzyme , gene
The receptor for the wilt‐inducing phytotoxin fusicoccin was purified to homogeneity from plasma membranes of Commelina communis as a complex with the radioligand [ 3 H]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 14‐3‐3 family, which comprises structurally conserved regulatory proteins of widespread occurrence and a wide range of functions. 14‐3‐3 isoform(s) constituting the fusicoccin receptor are distinguishable from other cellular 14‐3‐3 proteins by their tight association with the plasma membrane. Applying temperature‐induced Triton X‐114 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.