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MBE Advance Access published online on July 28, 2003
Molecular Biology and Evolution, doi:10.1093/molbev/msg205
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2003; all rights reserved
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Accepted June 21, 2003
© 2003 Society for Molecular Biology and Evolution

Original Articles

Early Vertebrate Evolution of the TATA-Binding Protein, TBP

Alla A. Bondareva 1 and Edward E. Schmidt 1*

1 Veterinary Molecular Biology, Marsh Labs, Montana State University, Bozeman, MT 59717

* To whom correspondence should be addressed. E-mail: eschmidt{at}montana.edu.


  Abstract

TBP functions in transcription initiation in all eukaryotes and in Archaebacteria. Although the 181 amino acid (a.a.) 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 non-therian tetrapods suggests that this domain also has more primitive functions. To gain insights into the pre-therian functions of the N terminus, we investigated its phylogenetic distribution. TBP cDNAs were isolated from representative non-tetrapod jawed vertebrates (zebrafish and shark), from more primitive jawless vertebrates (lamprey and hagfish), as well as from a pre-vertebrate 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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