Quantitation of protein phosphatase 1 and 2A in extracts of the budding yeast and fission yeast.
Serine/threonine protein phosphatases are also involved in the control of cell division. The aim of the present study was to compare the activity of protein phosphatase 1 (PP1) and 2A (PP2A) in cell extracts of the budding and fission yeast, made at different phases of growth. The activities of PP1 and PP2A toward phosphorylase were similar in extracts of S. cerevisiae. In S. pombe extracts, PP1 was responsible for more than 80% of the phosphorylase phosphatase activity. Ammonium sulfate-ethanol treatment increased the specific activity of the phosphatases and the percentage of PP2A in S. cerevisiae extracts. No increase in the proportion of PP2A was observed upon the same treatment of S. pombe extracts. The above results were confirmed by fractionation of PP1 and PP2A activities on a heparin-Sepharose column. The proportion of PP1 and PP2A activities did not change significantly during exponential cell growth but cells from stationary phase exhibited lower phosphatase activities. These results may indicate a lower level of expression of the PP2A genes in S. pombe and/or differences in the structure of the holoenzymes or their regulators in the two genera.
Farkas
I
I
Department of Medical Chemistry, University School of Medicine, Debrecen, Hungary.
Bakó
E
E
Murányi
A
A
Zeke
T
T
Sipiczki
M
M
Gergely
P
P
D002455:Cell Division / Q000502:physiology; D007527:Isoenzymes / Q000032:analysis*; D010749:Phosphoprotein Phosphatases / Q000032:analysis*; D054645:Protein Phosphatase 1; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000254:growth & development; D012568:Schizosaccharomyces / Q000201:enzymology* / Q000254:growth & development; D013045:Species Specificity; D013379:Substrate Specificity
D007527:Isoenzymes; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1