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Science 23 April 1993:
Vol. 260. no. 5107, pp. 530 - 533
DOI: 10.1126/science.8475383
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Articles

Science, Vol 260, Issue 5107, 530-533
Copyright © 1993 by American Association for the Advancement of Science

articles

Molecular basis for specific recognition of both RNA and DNA by a zinc finger protein

KR Clemens, V Wolf, SJ McBryant, P Zhang, X Liao, PE Wright, and JM Gottesfeld

Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.

Transcription factor IIIA (TFIIIA) from Xenopus oocytes binds both the internal control region of the 5S ribosomal RNA genes and the 5S RNA transcript itself. The nucleic acid binding domain of TFIIIA contains nine tandemly repeated zinc finger motifs. A series of precisely truncated forms of this protein have been constructed and assayed for 5S RNA and DNA binding. Different sets of zinc fingers were found to be responsible for high affinity interactions with RNA and with DNA. These results explain how a single protein can exhibit equal affinities for these two very different nucleic acids.


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A zinc finger directory for high-affinity DNA recognition.
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Analysis of the Binding of Xenopus Transcription Factor IIIA to Oocyte 5 S rRNA and to the 5 S rRNA Gene.
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Analysis of the Binding of Xenopus Ribosomal Protein L5 to Oocyte 5 S rRNA.
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The Interaction of TFIIIA with Specific RNA-DNA Heteroduplexes.
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