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The phosphorylation and the cytosolic-nuclear transport of nucleosome-associated, chromatin template proteins, e.g. histones, and of non-nucleosomal, non-chromatin template proteins, e.g. high mobility group (HMG) 1 and 2 proteins were examined in U373 cells. The phosphorylation pattern of histones separated in two-dimensional gels differed for the three H4 forms of H4 with the number of serine residues being 1 for the modified histones, 4 for the monophosphorylated species, and 5 for the polyphosphorylated species. HMG-1 and HMG-2 non-nucleosomal proteins were present in the nuclei of the U373 cells where they could be found in the form of an oligomeric complex. However, HMG-1 and HMG-2 proteins did not possess the ability to translocate in a cytosolic-nuclear shuttling system because they could not be taken up into nuclei upon a 2-h incubation in the presence of specific transport factors which we have previously shown to be necessary for this in vitro. The HMG-1 and