Molecular basis for specific recognition of both RNA and DNA by a zinc finger protein.
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.
Clemens
K R
KR
Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.
Wolf
V
V
McBryant
S J
SJ
Zhang
P
P
Liao
X
X
Wright
P E
PE
Gottesfeld
J M
JM
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D005260:Female; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D009865:Oocytes / Q000737:chemistry; D012341:RNA, Ribosomal, 5S / Q000378:metabolism*; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism*; D014981:Xenopus; D016335:Zinc Fingers / Q000502:physiology*
D004268:DNA-Binding Proteins; D012341:RNA, Ribosomal, 5S; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors; D004247:DNA