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MBE Advance Access originally published online on July 28, 2003
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Mol. Biol. Evol. 20(11):1932-1939. 2003
DOI: 10.1093/molbev/msg205
© 2003 by the Society for Molecular Biology and Evolution. ISSN: 0737-4038

Early Vertebrate Evolution of the TATA-Binding Protein, TBP

Alla A. Bondareva and Edward E. Schmidt

Veterinary Molecular Biology, Marsh Labs, Montana State University

E-mail: eschmidt{at}montana.edu.

TBP functions in transcription initiation in all eukaryotes and in Archaebacteria. Although the 181–amino acid (aa) carboxyl (C-) terminal core of the protein is highly conserved, TBP proteins from different phyla exhibit diverse sequences in their amino (N-) terminal region. In mice, the TBP N-terminus plays a role in protecting the placenta from maternal rejection; however the presence of similar TBP N-termini in nontherian tetrapods suggests that this domain also has more primitive functions. To gain insights into the pretherian functions of the N-terminus, we investigated its phylogenetic distribution. TBP cDNAs were isolated from representative nontetrapod jawed vertebrates (zebrafish and shark), from more primitive jawless vertebrates (lamprey and hagfish), and from a prevertebrate cephalochordate (amphioxus). Results showed that the tetrapod N-terminus likely arose coincident with the earliest vertebrates. The primary structures of vertebrate N-termini indicates that, historically, this domain has undergone events involving intragenic duplication and modification of short oligopeptide-encoding DNA sequences, which might have provided a mechanism of de novo evolution of this polypeptide.

Key Words: transcription • TFIID • cyclostome • minisatellite duplication • polypeptide genesis


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