HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 8, 6168-6174, February 21, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/8/6168    most recent M211205200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Schmidt, E. E. Articles by Capecchi, M. R. Search for Related Content PubMed PubMed Citation Articles by Schmidt, E. E. Articles by Capecchi, M. R. Social Bookmarking                      What's this?

Fundamental Cellular Processes Do Not Require Vertebrate-specific Sequences within the TATA-binding Protein^*

Edward E. Schmidt^§, Alla A. Bondareva, Jay R. Radke^¶, and Mario R. Capecchi

From the  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, tbp^N, which lacks 111 of 135 N-terminal amino acid residues. Most tbp^N/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 +/+, N/+, and N/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.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				J. R. Prigge and E. E. Schmidt Interaction of Protein Inhibitor of Activated STAT (PIAS) Proteins with the TATA-binding Protein, TBP J. Biol. Chem., May 5, 2006; 281(18): 12260 - 12269. [Abstract] [Full Text] [PDF]

				Z. Jallow, U. G. Jacobi, D. L. Weeks, I. B. Dawid, and G. J. C. Veenstra Specialized and redundant roles of TBP and a vertebrate-specific TBP paralog in embryonic gene regulation in Xenopus PNAS, September 14, 2004; 101(37): 13525 - 13530. [Abstract] [Full Text] [PDF]

				A. A. Bondareva and E. E. Schmidt Early Vertebrate Evolution of the TATA-Binding Protein, TBP Mol. Biol. Evol., November 1, 2003; 20(11): 1932 - 1939. [Abstract] [Full Text] [PDF]