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Because the phosphorylation of non-histone proteins has been suggested to play a role in the regulation of eukaryotic gene transcription, we have compared the phosphorylation of these proteins in normal and SV-40 transformed WI-38 human diploid fibroblasts. The rate of phosphorylation was found to be roughly ten-fold higher in the transformed cells, and this striking difference could not be accounted for by either an increased rate of phosphate transport or by the synthesis of new species of non-histone proteins which subsequently become phosphorylated. To our knowledge this is the most dramatic alteration in non-histone protein phosphorylation ever described, and therefore may have important implications for our understanding of malignant transformation.
D E Pumo, and
G S Stein, and
L J Kleinsmith
July 1974,
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D E Pumo, and
G S Stein, and
L J Kleinsmith
March 1979,
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D E Pumo, and
G S Stein, and
L J Kleinsmith
August 1975,
Cancer research,
D E Pumo, and
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L J Kleinsmith
April 1975,
Life sciences,
D E Pumo, and
G S Stein, and
L J Kleinsmith
December 1976,
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D E Pumo, and
G S Stein, and
L J Kleinsmith
October 1969,
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D E Pumo, and
G S Stein, and
L J Kleinsmith
January 1977,
Proceedings of the National Academy of Sciences of the United States of America,
D E Pumo, and
G S Stein, and
L J Kleinsmith
June 1972,
The Journal of biological chemistry,
D E Pumo, and
G S Stein, and
L J Kleinsmith
December 1998,
Molecules and cells,
D E Pumo, and
G S Stein, and
L J Kleinsmith
July 1969,
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