Electron microscopy reveals that transcription factor TFIIIA bends 5S DNA.
We have used a high-resolution analytical electron microscopic technique, electron spectroscopic imaging, to study the in vitro interaction between the transcription factor IIIA (TFIIIA) and 5S ribosomal gene DNA. The images and analytical measurements support our proposal that the helix axis is bent by the protein into a hairpin-shaped configuration.
Bazett-Jones
D P
DP
Department of Medical Biochemistry, University of Calgary, Alberta, Canada.
Brown
M L
ML
D000818:Animals; D002417:Cattle; D004275:DNA, Ribosomal / Q000648:ultrastructure*; D004268:DNA-Binding Proteins / Q000378:metabolism; D005796:Genes; D008854:Microscopy, Electron; D009690:Nucleic Acid Conformation; D010063:Ovum / Q000166:cytology; D012335:RNA, Ribosomal / Q000648:ultrastructure*; D012341:RNA, Ribosomal, 5S / Q000648:ultrastructure*; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors / Q000648:ultrastructure*; D014982:Xenopus laevis
D004275:DNA, Ribosomal; D004268:DNA-Binding Proteins; D012335:RNA, Ribosomal; D012341:RNA, Ribosomal, 5S; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors