Hislone HI acts as a general repressor of transcription in eukaryotcs by organizing nueleosomcs into inaccessible condensed forms of chromatin, The capability of HI to bind to DNA with some sequence specificity is Likely to be critical in the control of tl~cse processes. We show I,¢re thai ATP and several other nu¢leotides, including non-hydrolyzable derivatives, can inhibit DNA binding of HI. The results also show thal ATP differentially affects binding of HI to DNA in a fashion enhancing nu¢leotide sequen¢~ specificity of the binding. The study suggests a novel mechanism of modulation of H1 activity that has important implications for lhe role of HI as a traa~:riptional regulator.
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