A new approach to the analysis of DNase I footprinting data and its application to the TFIIIA/5S DNA complex.
We have re-examined DNase I footprinting data for the binding of transcription factor IIIA (TFIIIA) to the 5S RNA gene, taking into account the protein-DNA contacts observed in the crystal structure of the DNase I/DNA complex (1, 2). This structure was not available when many of the original footprinting experiments on the TFIIIA/DNA complex were performed. In this way the pattern of DNase I cleavage can be interpreted to map out with greater precision the regions on the 5S DNA occupied by TFIIIA. Then, assuming the binding site for a zinc-finger may be the same as that found in the structure of the zinc-finger protein Zif268/DNA complex (3), and taking into account footprinting data for truncated forms of TFIIIA, the TFIIIA zinc-fingers were fitted within the permitted regions. On the basis of this, an alignment of the zinc-fingers of TFIIIA with its DNA binding site is proposed, which combines features of earlier models (4).
Fairall
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MRC Laboratory of Molecular Biology, Cambridge, UK.
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D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D004275:DNA, Ribosomal / Q000378:metabolism*; D003850:Deoxyribonuclease I; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D012341:RNA, Ribosomal, 5S / Q000235:genetics*; D017384:Sequence Deletion; D013379:Substrate Specificity; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors / Q000378:metabolism*; D014982:Xenopus laevis; D016335:Zinc Fingers
D004275:DNA, Ribosomal; D012341:RNA, Ribosomal, 5S; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors; D003850:Deoxyribonuclease I