The DNA binding site of the Xenopus transcription factor IIIA has a non-B-form structure.
On the basis of nuclease digestion studies we proposed that the DNA binding site of transcription factor IIIA (TFIIIA) may have an overall structure with A-type rather than B-type characteristics. This proposal was substantiated by the crystal structure of a part of the TFIIIA binding site. Recently, however, it has been reported that the binding site for TFIIIA is B-form in solution, thus implying that the conformation present in crystals is not the structure in solution. We have carried out a study using comparative circular dichroism (CD) spectroscopy of a number of double stranded deoxyoligonucleotides of different sequence, and known crystal structure. The correlation we have found between CD characteristics and certain structural parameters indicates that the solution and crystal structures of the TFIIIA binding site are closely related. This structure may be classed as an intermediate type, between A-form and B-form DNA.
MRC Laboratory of Molecular Biology, Cambridge, London, UK.
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D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002942:Circular Dichroism; D003460:Crystallization; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism; D015394:Molecular Structure; D009690:Nucleic Acid Conformation; D012996:Solutions; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors / Q000378:metabolism*; D014981:Xenopus
D004268:DNA-Binding Proteins; D012996:Solutions; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors; D004247:DNA