Identification, Molecular Cloning, and Characterization of the Sixth Subunit of Human Transcription Factor TFIIIC

TFIIIC in yeast and humans is required for transcription of tRNA and 5 S RNA genes by RNA polymerase III. In the yeast Saccharomyces cerevisiae, TFIIIC is composed of six subunits, five of which are conserved in humans. We report the identification, molecular cloning, and characterization of the six...

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Published in:The Journal of biological chemistry 2007-06, Vol.282 (23), p.17179-17189
Main Authors: Dumay-Odelot, Hélène, Marck, Christian, Durrieu-Gaillard, Stéphanie, Lefebvre, Olivier, Jourdain, Sabine, Prochazkova, Martina, Pflieger, Aude, Teichmann, Martin
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Cloning, Molecular
DNA Primers
Fluorescent Antibody Technique
Humans
Molecular Sequence Data
Phylogeny
Recombinant Proteins - chemistry
Recombinant Proteins - classification
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
RNA Polymerase III - metabolism
Saccharomyces cerevisiae
Sequence Homology, Amino Acid
Transcription Factors, TFIII - chemistry
Transcription Factors, TFIII - classification
Transcription Factors, TFIII - genetics
Transcription Factors, TFIII - metabolism
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Summary:TFIIIC in yeast and humans is required for transcription of tRNA and 5 S RNA genes by RNA polymerase III. In the yeast Saccharomyces cerevisiae, TFIIIC is composed of six subunits, five of which are conserved in humans. We report the identification, molecular cloning, and characterization of the sixth subunit of human TFIIIC, TFIIIC35, which is related to the smallest subunit of yeast TFIIIC. Human TFIIIC35 does not contain the phosphoglycerate mutase domain of its yeast counterpart, and these two proteins display only limited homology within a 34-amino acid domain. Homologs of the sixth TFIIIC subunit are also identified in other eukaryotes, and their phylogenic evolution is analyzed. Affinity-purified human TFIIIC from an epitope-tagged TFIIIC35 cell line is active in binding to and in transcription of the VA1 gene in vitro. Furthermore, TFIIIC35 specifically interacts with the human TFIIIC subunits TFIIIC63 and, to a lesser extent, TFIIIC90 in vitro. Finally, we determined a limited region in the smallest subunit of yeast TFIIIC that is sufficient for interacting with the yeast TFIIIC subunit ScTfc1 (orthologous to TFIIIC63) and found it to be adjacent to and overlap the 34-amino acid domain that is conserved from yeast to humans.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M611542200