Abstract
Transcription of eukaryotic transfer RNA genes involves, as a primary event, the stable binding of a protein factor to the intragenic promoter1–4. The internal control region is composed of two non-contiguous conserved sequence elements, the A and B blocks. These are variably spaced depending on the genes5–8. τ, a large transcription factor purified from yeast cells4, interacts with these two control elements as shown by DNase I footprinting, exonuclease digestion, dimethyl sulphate protection experiments9,10 and by analysis of point mutations. Here we used a limited proteolysis treatment to obtain a smaller form of τ with drastically altered DNA binding properties. A protease-resistant domain interacts solely with the B block region of tRNA genes.
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Marzouki, N., Camier, S., Ruet, A. et al. Selective proteolysis defines two DNA binding domains in yeast transcription factor τ. Nature 323, 176–178 (1986). https://doi.org/10.1038/323176a0
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DOI: https://doi.org/10.1038/323176a0
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