Ouhammouch, Mohamed and Hausner, Winfried and Geiduschek, E. Peter (2009) TBP domain symmetry in basal and activated archaeal transcription. MOLECULAR MICROBIOLOGY, 71 (1). pp. 123-131. ISSN 0950-382X, 1365-2958
Full text not available from this repository. (Request a copy)Abstract
The TATA box binding protein (TBP) is the platform for assembly of archaeal and eukaryotic transcription preinitiation complexes. Ancestral gene duplication and fusion events have produced the saddle-shaped TBP molecule, with its two direct-repeat subdomains and pseudo-two-fold symmetry. Collectively, eukaryotic TBPs have diverged from their present-day archaeal counterparts, which remain highly symmetrical. The similarity of the N- and C-halves of archaeal TBPs is especially pronounced in the Methanococcales and Thermoplasmatales, including complete conservation of their N- and C-terminal stirrups; along with helix H'1, the C-terminal stirrup of TBP forms the main interface with TFB/TFIIB. Here, we show that, in stark contrast to its eukaryotic counterparts, multiple substitutions in the C-terminal stirrup of Methanocaldococcus jannaschii (Mja) TBP do not completely abrogate basal transcription. Using DNA affinity cleavage, we show that, by assembling TFB through its conserved N-terminal stirrup, Mja TBP is in effect ambidextrous with regard to basal transcription. In contrast, substitutions in either its N- or the C-terminal stirrup abrogate activated transcription in response to the Lrp-family transcriptional activator Ptr2.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TATA-BINDING PROTEIN; CELL-FREE TRANSCRIPTION; PREINITIATION COMPLEX; CRYSTAL-STRUCTURE; DNA-BINDING; STRUCTURAL BASIS; RNA-POLYMERASE; MINOR-GROOVE; FACTOR IIB; IN-VIVO; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) > Prof. Dr. Dina Grohmann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 13 Oct 2020 14:44 |
| Last Modified: | 13 Oct 2020 14:44 |
| URI: | https://pred.uni-regensburg.de/id/eprint/29809 |
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