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Phosphorylation affects the DNA affinity of the nuclear protein 24/7 from human tumor cells
Author(s) -
Radtke Janna,
Unteregger Gerhard
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80057-7
Subject(s) - phosphorylation , dna , chemistry , microbiology and biotechnology , protein phosphorylation , nuclear protein , biochemistry , biology , gene , transcription factor , protein kinase a
In the present study we investigated the binding behavior of nuclear proteins from human tumor cells to human placental DNA coupled on CNBr‐activated Sepharose. When nuclear proteins soluble in 5 M urea prepared from serum‐stimulated cells and containing the majority of the nonhistone proteins were applied onto a dsDNA column, next to several other proteins one prominent group consisting of at least 2 distinct proteins with a p I at 7 and a molecular mass near 24 kDa bound to DNA. The DNA‐binding ability of one of them is lost on phosphorylation and is recovered after dephosphorylation using alkaline phosphatase. Additionally, normal human fibroblasts taken as controls exhibit comparatively low levels of these 24/7 proteins, indicating a particular function in tumor cells.