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Isolation of TFC1, A Gene Encoding Of Two DNA-Binding Subunits of Yeast Transcription Factor τ (TFIIIC)
Robert N. Swanson, Christine Conesa, Olivier Lefebvre, Christophe Carles, Anny Ruet, Eric Quemeneur, Jean Gagnon and Andre Sentenac
Proceedings of the National Academy of Sciences of the United States of America
Vol. 88, No. 11 (Jun. 1, 1991), pp. 4887-4891
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2357159
Page Count: 5
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Transcription factor TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. The factor from Saccharomyces cerevisiae, also called τ, is a large, multisubunit protein (550-650 kDa) containing two polypeptides that interact directly with DNA encoding tRNA (tDNA). We have obtained peptide sequences from the 95-kDa DNA-binding subunit (τ95) and cloned the corresponding gene, called TFC1. The gene encodes a polypeptide of calculated Mr 73,500. However, when TFC1 was transcribed and translated in vitro, the gene product comigrated with τ95 in SDS/polyacrylamide gels. A fusion protein expressed in bacteria was able to prevent the binding of anti-τ95 antibodies to τ-tDNA complexes. The TFC1 gene is present in single copy on yeast chromosome II and is essential for growth. Spores containing a disrupted gene germinate but only proceed through a few cell divisions before ceasing to grow. The TFC1-encoded protein contains a potential helix-turn-helix structure and an acidic carboxyl-terminal domain, a feature characteristic of some DNA-binding proteins and transcriptional regulators.
Proceedings of the National Academy of Sciences of the United States of America © 1991 National Academy of Sciences