A protein-protein interaction is essential for stable complex formation on a 5 S RNA gene.
Stable complex formation on a Xenopus somatic 5 S RNA gene requires protein-protein interactions between the non-DNA binding domain of transcription factor (TF) IIIA and activities in a TFIIIC fraction. No significant changes in the structure of the TFIIIA.DNA complex can be detected as a consequence of stabilization, indicating that protein confirmation is the primary determinant of stability.
Hayes
J
J
Department of Chemistry, Johns Hopkins University, Baltimore, Maryland 21218.
Tullius
T D
TD
Wolffe
A P
AP
D000818:Animals; D004275:DNA, Ribosomal / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D005786:Gene Expression Regulation; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D012335:RNA, Ribosomal / Q000235:genetics*; D012341:RNA, Ribosomal, 5S / Q000235:genetics*; D012045:Regulatory Sequences, Nucleic Acid; D013329:Structure-Activity Relationship; D013696:Temperature; D014157:Transcription Factors / Q000378:metabolism*; D014158:Transcription, Genetic; D014982:Xenopus laevis
D004275:DNA, Ribosomal; D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D012335:RNA, Ribosomal; D012341:RNA, Ribosomal, 5S; D014157:Transcription Factors