Effect of serine/threonine protein kinases and protein phosphatases inhibitors on mitosis progression in a synchronized tobacco BY-2 culture |
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| Authors: | Ya A Sheremet A I Emets A Azmi K Vissenberg J -P Verbelen Ya B Blume |
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| Institution: | 1.Institute of Food Biotechnology and Genomics,National Academy of Sciences of Ukraine,Kiev,Ukraine;2.University of Antwerp,Antwerpen,Belgium |
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| Abstract: | In order to investigate the role of various serine/threonine protein kinases and protein phosphatases in the regulation of
mitosis progression in plant cells, the influence of cyclin(olomoucine) and Ca2+/calmodulin-dependent (W7) protein kinases inhibitors, as well as protein kinase C inhibitors (H7 and staurosporine), and
a protein phosphatases inhibitor (okadaic acid) on mitosis progression in synchronized tobacco BY-2 cells has been studied.
It was found that BY-2 culture treatment with inhibitors of cyclin-dependent protein kinases and protein kinase C caused a
prophase delay, reduced the mitotic index, and displaced the mitotic peak as compared with control cells. Inhibition of Ca2+/calmodulin-dependent protein kinases enhanced the cells entry into prophase and delayed their exit from mitosis. Meanwhile
inhibition of serine/threonine protein phosphatases insignificantly enhances synchronized BY-2 cells entering into all phases
of mitosis. |
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