Relief of YY1-induced transcriptional repression by protein-protein interaction with the nucleolar phosphoprotein B23

• Published in: The Journal of biological chemistry Vol. 269; no. 9; pp. 6506 - 6510
• Main Authors: INOUYE, C. J, SETO, E
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 04-03-1994
• Subjects: Animals; Biological and medical sciences; Cell Nucleolus - metabolism; Cloning, Molecular; DNA, Complementary - isolation & purification; DNA, Complementary - metabolism; DNA-Binding Proteins - biosynthesis; DNA-Binding Proteins - isolation & purification; DNA-Binding Proteins - metabolism; Erythroid-Specific DNA-Binding Factors; Escherichia coli - metabolism; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation; HeLa Cells; Humans; Mice; Molecular and cellular biology; Molecular genetics; Nuclear Proteins - biosynthesis; Nuclear Proteins - isolation & purification; Nuclear Proteins - metabolism; Phosphoproteins - metabolism; Protein Binding; Protein Biosynthesis; Saccharomyces cerevisiae; Transcription Factors - biosynthesis; Transcription Factors - isolation & purification; Transcription Factors - metabolism; Transcription, Genetic; Transcription. Transcription factor. Splicing. Rna processing; Transfection; YY1 Transcription Factor; Vertebrata; Mammalia; Mouse; Phosphoproteins; Rodentia; Molecular association; Transcription repressor; Nucleolus; Transcription factor
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(17)37400-8

Previous studies have shown that the transcription factor YY1 can both activate and repress transcription of many mammalian
genes (reviewed by Hahn (Hahn, S. (1992) Curr. Biol. 2, 152-154)). Given the diverse effects of the YY1 protein, it seems
likely that its function depends on interaction with other cellular factors. We have used the yeast two-hybrid system to isolate
mouse cDNAs encoding proteins capable of directly binding to YY1. Sequence analysis of one clone revealed it had an open reading
frame with the potential to code for a protein nearly identical to the previously published mouse nucleolar phosphoprotein
B23. The YY1.B23 complex is specific, and occurs in vivo and in vitro. Overexpression of the B23 protein can reverse the transcriptional
repression exerted by YY1. These results suggest a role for a nucleolar protein as a component in transcription and provide
a possible mechanism for transcriptional regulation by YY1.