Identification of a phosphatase activity, toward the phosphopeptide pyroGlu-Asp-Asp-Ser(p)-Asp-Glu-Glu-Asn, in nuclear extract from HL-60 promyelocitic leukaemia cells

Identification of a phosphatase activity, toward the phosphopeptide pyroGlu-Asp-Asp-Ser(p)-Asp-Glu-Glu-Asn, in nuclear extract from HL-60 promyelocitic leukaemia cells

Total protein extract from HL-60 cells was found to be able to dephosphorylate the RNA polymerase II octapeptide pyroGlu-Asp-Asp-Ser-Asp-Glu-Glu-Asn previously phosphorylated with protein kinase CKII (pCKII). Fractionation in cytoplasm, nuclear and chromatin extracts shows the phosphatase activity t...

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Veröffentlicht in:Physiological chemistry and physics and medical NMR 2000, Vol.32 (1), p.27-33
Hauptverfasser: Cardellini, E, Nardicchi, V, Macchioni, L
Format: Artikel
Sprache:eng
Schlagworte:
Casein Kinase II - chemistry
Cell Extracts - chemistry
Enzyme Activation
HL-60 Cells
Humans
Neoplasm Proteins - analysis
Neoplasm Proteins - chemistry
Nuclear Proteins - analysis
Nuclear Proteins - chemistry
Phosphopeptides - chemistry
Phosphorylation
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Zusammenfassung:Total protein extract from HL-60 cells was found to be able to dephosphorylate the RNA polymerase II octapeptide pyroGlu-Asp-Asp-Ser-Asp-Glu-Glu-Asn previously phosphorylated with protein kinase CKII (pCKII). Fractionation in cytoplasm, nuclear and chromatin extracts shows the phosphatase activity to be localized only in the nucleus, but not to be bound to the chromatin.
ISSN:0748-6642