Abstract
A 41,000 protein, p41, was highly purified from human promyelocytic HL-60 cells by chromatography on GTP-agarose columns. The purified p41 inhibited phosphorylation of endogenous substrates present in partially purified DNA-PK from HL-60 or HeLa cells, as well as phosphorylation of recombinant protein tau mediated by the purified HeLa DNA-PK. The ability of p41 to inhibit DNA-PK was largely abolished by heating at 95 degrees C for 30 min.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Chromatography, Affinity
-
DNA / physiology*
-
DNA-Activated Protein Kinase
-
DNA-Binding Proteins*
-
Electrophoresis, Polyacrylamide Gel
-
HeLa Cells
-
Humans
-
Nuclear Proteins
-
Phosphorylation
-
Protein Serine-Threonine Kinases / antagonists & inhibitors*
-
Proteins / isolation & purification
-
Proteins / physiology*
-
Tumor Cells, Cultured
Substances
-
DNA-Binding Proteins
-
Nuclear Proteins
-
Proteins
-
DNA
-
DNA-Activated Protein Kinase
-
PRKDC protein, human
-
Protein Serine-Threonine Kinases