lAA and BAP affect protein phosphorylation-dependent processes during sucrose-mediated G1 to S and G2 to M transitions in root meristem cells of Vicia faba

• Main Authors: Justyna Teresa Polit, Janusz Maszewski, Marzena Rosiak
• Format: Article
• Language: English
• Published: Polish Botanical Society 2011-01-01
• Series: Acta Societatis Botanicorum Poloniae
• Subjects: protein phosphorylation; sucrose; auxin; cytokinin; control points of cell cycle; Vicia faba
• Online Access: https://pbsociety.org.pl/journals/index.php/asbp/article/view/49

In carbohydrate-starved root meristems of Vicia faba subsp. minor, the expression of two Principal Control Points located at the final stages of the G1 (PCP1) and G2 (PCP2) phases has been found to be correlated with a marked decrease of protein phosphorylation within cell nuclei, nucleoli and cytoplasm. Adopting the same experimental model in our present studies, monoclonal FITC conjugated antibodies that recognize phosphorylated form of threonine (αTPab-FITC) were used to obtain an insight about how the indole-3-acetic acid (IAA), benzyl-6-aminopurine (BAP), and the mixture of both phytohormones influence the time-course changes in an overall protein phosphorylation during sucrose-mediated PCP1→S and PCP2→M transitions. Unsuspectedly, neither IAA, BAP, nor the mixture of both phytohormones supplied in combination with sucrose did up-regulate protein phosphorylation. However using the block-and-release method, it was shown that root meristems of Vicia provided with sucrose alone indicated higher levels of αTPab-FITC. Contrarily, phytohormones supplied in combination with sucrose induced apparent decline in phosphorylation of cell proteins, which - when compared with the influence of sucrose alone - became increasingly evident in time. Thus, it seems probable, that a general decline in the amount of αTPab-FITC labeled epitopes may overlay specific phosphorylations and dephosphorylations governed by the main cell cycle kinases and phosphatases.