Plant cell pH‐static circuit mediated by fusicoccin‐binding proteins

FEBS Letters

Trofimova, Marina S³  Drabkin, Artem V²  Chelysheva, Vera V²  Smolenskaya, Irina N³  Babakov, Alexey V²  Klychnikov, Oleg I¹ 

[1] Department of Biotechnology, Timiryazev Agricultural Academy, 49 Timiryazevskaya St., Moscow 127550, Russia;Institute of Agricultural Biotechnology, Russian Academy of Agricultural Sciences, 42 Timiryazevskaya St., Moscow 127550, Russia;Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, 35 Botanicheskaya St., Moscow 127276, Russia

关键词: Protoplast;    Fusicoccin;    Fusicoccin-binding protein;    Cytoplasmic pH;    Affinity;   

DOI  :  10.1016/S0014-5793(97)00172-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

On sugar beet protoplasts that carry two types of fusicoccin-binding sites, a pH downshift in a physiological range (7.0–6.6) markedly enhanced the efficiency of fusicoccin (FC) binding, mainly owing to increased avidity of low-affinity FC-binding sites. This may allow the FC-binding proteins to act as pH-sensitive modulators of cell activity, for instance, via plasma membrane H⁺-ATPase or potassium channels. © 1997 Federation of European Biochemical Societies

【 授权许可】

Unknown