The phosphorylation of nuclear proteins in normal and transformed cells.

F. Gabrielli, Sara Courtneidge

Research output: Contribution to journalArticle

Abstract

Normal (Rat 1) and transformed cells (middle T antigen-transformed derivative 3C3) were grown in the presence of 32P-orthophosphate. 32P-labelled nuclear proteins were fractionated by means of two-dimensional gel electrophoresis and detected by autoradiography. The comparative analysis of the autoradiographs of the normal and transformed cells revealed differences in the phosphorylation patterns of histone and low-molecular-mass high mobility group proteins (HMG). Three of the HMG proteins were highly phosphorylated in the transformed cells, and the analysis of their phosphorylation sites showed that these HMG proteins were phosphorylated on serine and threonine but not on tyrosine residues.

Original languageEnglish (US)
Pages (from-to)9-15
Number of pages7
JournalItalian Journal of Biochemistry
Volume41
Issue number1
StatePublished - Jan 1992
Externally publishedYes

Fingerprint

High Mobility Group Proteins
Phosphorylation
Nuclear Proteins
Viral Tumor Antigens
Electrophoresis, Gel, Two-Dimensional
Molecular mass
Threonine
Electrophoresis
Autoradiography
Histones
Serine
Tyrosine
Rats
Proteins
Gels
Phosphates
Derivatives

ASJC Scopus subject areas

  • Biochemistry

Cite this

The phosphorylation of nuclear proteins in normal and transformed cells. / Gabrielli, F.; Courtneidge, Sara.

In: Italian Journal of Biochemistry, Vol. 41, No. 1, 01.1992, p. 9-15.

Research output: Contribution to journalArticle

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