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Originally published In Press as doi:10.1074/jbc.M211205200 on December 5, 2002

J. Biol. Chem., Vol. 278, Issue 8, 6168-6174, February 21, 2003
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Fundamental Cellular Processes Do Not Require Vertebrate-specific Sequences within the TATA-binding Protein*

Edward E. SchmidtDagger §, Alla A. BondarevaDagger , Jay R. RadkeDagger , and Mario R. Capecchi||

From the Dagger  Department of Veterinary Molecular Biology, Marsh Laboratories, Montana State University, Bozeman, Montana 59717 and the || Howard Hughes Medical Institute, Eccles Institute of Human Genetics, University of Utah, Salt Lake City, Utah 84112-5331

The 180-amino acid core of the TATA-binding protein (TBPCORE) is conserved from Archae bacteria to man. Vertebrate TBPs contain, in addition, a large and highly conserved N-terminal region that is not found in other phyla. We have generated a line of mice in which the tbp allele is replaced with a version, tbpDelta N, which lacks 111 of 135 N-terminal amino acid residues. Most tbpDelta N/Delta N fetuses die in midgestation. To test whether a disruption of general cellular processes contributed to this fetal loss, primary fibroblast cultures were established from +/+, Delta N/+, and Delta N/Delta N fetuses. The cultures exhibited no genotype-dependent differences in proliferation or in expression of the proliferative markers dihydrofolate reductase (DHFR) mRNA (S phase-specific) and cdc25B mRNA (G2-specific). The mutation had no effect on transcription initiation site fidelity by either RNA polymerase II (pol II) or pol III. Moreover, the mutation did not cause differences in levels of U6 RNA, a pol III-dependent component of the splicing machinery, in mRNA splicing efficiency, in expression of housekeeping genes from either TATA-containing or TATA-less promoters, or in global gene expression. Our results indicated that general eukaryotic cell functions are unaffected by deletion of these vertebrate-specific sequences from TBP. Thus, all activities of this polypeptide domain must either be compensated for by redundant activities or be restricted to situations that are not represented by primary fibroblasts.

* This work was supported by grants from the March of Dimes Foundation, National Institutes of Health, National Science Foundation, and USDA Animal Health Funds (to E. E. S.) and by awards from the Howard Hughes Medical Institute and the Mathers Charitable Foundation (to M. R. C.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Funded as a Basil O'Connor New Investigator of the March of Dimes Foundation, a Howard Hughes Medical Institute Fellow of the Life Sciences Research Foundation, and as an Investigator of the Montana Agricultural Experiment Station. To whom correspondence should be addressed. E-mail: eschmidt@montana.edu.

Supported by a postdoctoral fellowship from the USDA and by an appointment in the laboratory of M. W. White.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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