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Plant cell pH‐static circuit mediated by fusicoccin‐binding proteins
Author(s) -
Drabkin Artem V,
Trofimova Marina S,
Smolenskaya Iri,
Klychnikov Oleg I,
Chelysheva Vera V,
Babakov Alexey V
Publication year - 1997
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/s0014-5793(97)00172-5
Subject(s) - fusicoccin , chemistry , cell , biophysics , biochemistry , microbiology and biotechnology , biology , enzyme , atpase
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