Activation of beta-Glucan Synthases by Wall-Bound Purple Acid Phosphatase in Tobacco Cells
2009 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 150, no 4, 1822-1830 p.Article in journal (Refereed) Published
Wall-bound purple acid phosphatases have been shown to be potentially involved in the regulation of plant cell growth. The aim of this work was to further investigate the function of one of these phosphatases in tobacco (Nicotiana tabacum), NtPAP12, using transgenic cells overexpressing the enzyme. The transgenic cells exhibited a higher level of phosphatase activity in their walls. The corresponding protoplasts regenerating a cell wall exhibited a higher rate of beta-glucan synthesis and cellulose deposition was increased in the walls of the transgenic cells. A higher level of plasma membrane glucan synthase activities was also measured in detergent extracts of membrane fractions from the transgenic line, while no activation of Golgi-bound glycan synthases was detected. Enzymatic hydrolysis and methylation analysis were performed on the products synthesized in vitro by the plasma membrane enzymes from the wild-type and transgenic lines extracted with digitonin and incubated with radioactive UDP-glucose. The data showed that the glucans consisted of callose and cellulose and that the amount of each glucan synthesized by the enzyme preparation from the transgenic cells was significantly higher than in the case of the wildtype cells. The demonstration that callose and cellulose synthases are activated in cells overexpressing the wall-bound phosphatase NtPAP12 suggests a regulation of these carbohydrate synthases by a phosphorylation/dephosphorylation process, as well as a role of wall-bound phosphatases in the regulation of cell wall biosynthesis.
Place, publisher, year, edition, pages
2009. Vol. 150, no 4, 1822-1830 p.
callose synthase, plasma-membrane, cellulose biosynthesis, higher-plants, pollen tubes, udp-glucose, in-vitro, genes, phosphorylation, protoplasts
IdentifiersURN: urn:nbn:se:kth:diva-18661DOI: 10.1104/pp.109.139287ISI: 000268692200020ScopusID: 2-s2.0-68249157006OAI: oai:DiVA.org:kth-18661DiVA: diva2:336708
QC 201005252010-08-052010-08-052011-02-10Bibliographically approved