Stimulation of acid invertase activity by indol-3yl-acetic acid in tissues undergoing cell expansion

The soluble acid invertase activity of young, excised P. vulgaris internodal segments fell when they were incubated in water, and their elongation ceased within 6–7 h. IAA (10 M) promoted segment elongation and stimulated an increase in the specific activity of acid invertase to a level greater than that originally present. The rate of segment elongation in the presence of IAA was closely and positively correlated with the specific activity of the enzyme. Optimum concentration of IAA for both elongation and stimulation of invertase activity was 10 M. Concurrent protein synthesis was necessary for these responses to IAA. Segments cut from mature, fully-elongated internodes did not responsd to IAA.Inclusion of Ca²⁺, vanadate or mannitol in the incubation medium abolished IAA-induced segment elongation but did not inhibit the stimulation of acid invertase activity by IAA. Auxin-induced elongation and acid invertase activity were both substantially increased in the presence of up to 25 mM D-glucose or up to 50 mM sucrose. Inclusion of either sugar in the medium considerably increased tissue hexose concentrations. Under some circumstances cell growth and invertase synthesis may compete for available hexose substrate.It is concluded that IAA-induced promotion of acid invertase in P. vulgaris internodal segments is not simply an indirect consequence of removal of end-product (hexose) during IAA-induced cell growth and that a more direct action of IAA on enzyme turnover is involved.