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

FEBS Letters

Eckerskorn, C.¹  Oecking, C.²  Weiler, E.W.² 

[1] Abteilung Proteinanalytik, Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany;Lehrstuhl für Pflanzenphysiologie, Ruhr-Universität, D-44780 Bochum, Germany

关键词: 14-3-3 Proteins;    Fusicoccin;    Fusicoccin receptor (identification);   

DOI  :  10.1016/0014-5793(94)00949-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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.

【 授权许可】

Unknown