The enzyme involved in sulfation of the turgorin, gallic acid 4-O-(β-d-glucopyranosyl-6'-sulfate) is pulvini-localized in Mimosa pudica

A sulfotransferase (ST) which catalyzes the transfer of sulfate from 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to gallic acid glucoside was characterized from microsomal preparations of Mimosa pudica. The product of the reaction was found to co-elute on HPLC with the periodic leaf movement factor 1 (PLMF-1) (gallic acid β-d -gluco-pyranosyl-6′-sulfate). The distribution of the enzyme activity was restricted to plasma membrane preparations from primary, secondary and tertiary pulvini. The M. pudica ST activity was inhibited in a dose-dependent manner in the presence of an antibody raised against the flavonol 3-sulfotransferase of Flaveria chloraefolia, suggesting structural similarities between the two proteins. Western blot analysis of M. pudica protein extracts using these antibodies indicated the presence of a cross-reactive polypeptide with an apparent molecular mass of 42 000 Da whose distribution correlates with the presence of the gallic acid glucoside ST activity. Indirect immunogold labeling of resin-embedded sections from tertiary pulvini showed a specific localization of gold particles on the sieve-tube plasma membranes. The label distribution was uniform and other cellular organelles and membrane systems displayed little or no labeling. The results of the Western blot and immunocytochemical studies are consistent with the detection of the gallic acid glucoside ST activity in plasma membrane preparations of M. pudica pulvini cells. The specific tissue distribution of the ST in motor organ phloem cells suggests that this is the site of synthesis and/or accumulation of PLMF-1 and supports the proposed hypothesis that PLMF-1 may be acting as a chemical signal during the seismonastic response of M. pudica.