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Evolutionary history of the TBP-domain superfamily

Brindefalk, B; Dessailly, BH; Yeats, C; Orengo, C; Werner, F; Poole, AM; (2013) Evolutionary history of the TBP-domain superfamily. Nucleic Acids Res , 41 (5) 2832-45+-2832-45+. 10.1093/nar/gkt045%20%5Bdoi%5D.

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Abstract

The TATA binding protein (TBP) is an essential transcription initiation factor in Archaea and Eucarya. Bacteria lack TBP, and instead use sigma factors for transcription initiation. TBP has a symmetric structure comprising two repeated TBP domains. Using sequence, structural and phylogenetic analyses, we examine the distribution and evolutionary history of the TBP domain, a member of the helix-grip fold family. Our analyses reveal a broader distribution than for TBP, with TBP-domains being present across all three domains of life. In contrast to TBP, all other characterized examples of the TBP domain are present as single copies, primarily within multidomain proteins. The presence of the TBP domain in the ubiquitous DNA glycosylases suggests that this fold traces back to the ancestor of all three domains of life. The TBP domain is also found in RNase HIII, and phylogenetic analyses show that RNase HIII has evolved from bacterial RNase HII via TBP-domain fusion. Finally, our comparative genomic screens confirm and extend earlier reports of proteins consisting of a single TBP domain among some Archaea. These monopartite TBP-domain proteins suggest that this domain is functional in its own right, and that the TBP domain could have first evolved as an independent protein, which was later recruited in different contexts.

Type: Article
Title: Evolutionary history of the TBP-domain superfamily
DOI: 10.1093/nar/gkt045%20%5Bdoi%5D
Publisher version: http://dx.doi.org/10.1093/nar/gkt045%20%5Bdoi%5D
Additional information: citeulike-article-id: 12411852 citeulike-linkout-0: http://dx.doi.org/10.1093/nar/gkt045%20%5Bdoi%5D comment: eng —=note-separator=— Nlm —=note-separator=— Brindefalk, Bjorn Dessailly, Benoit H Yeats, Corin Orengo, Christine Werner, Finn Poole, Anthony M BB/H019332/1/Biotechnology and Biological Sciences Research Council/United Kingdom WT096553MA/Wellcome Trust/United Kingdom Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov’t England Nucleic acids research Nucleic Acids Res. 2013 Mar 1;41(5):2832-45. doi: 10.1093/nar/gkt045. Epub 2013 Feb 1. —=note-separator=— Evolutionary history of the TBP-domain superfamily —=note-separator=— Mar 1 keywords: acid, amino, analysis, animals, archaeal, bacterial, binding, cluster, dna, dna-binding, evolution, genetic, genetics, glycosylases-chemistry-, homology, humans, models, molecular, phylogeny, protein, protein-chemistry-, proteins-chemistry-, proteins-chemistry-genetics, ribonucleases-chemistry-, secondary, sequence, structural, structure, tata-box, tertiary-genetics, *file-import-13-06-12 posted-at: 2013-06-12 22:01:28 priority: 2 bdsk-url-1: http://dx.doi.org/10.1093/nar/gkt045%5C%20%5C%5Bdoi%5C%5D bdsk-url-2: http://dx.doi.org/10.1093/nar/gkt045%5C%2520%5C%255Bdoi%5C%255D
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1396634
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