ArticleNucleic acids research2013
Evolutionary history of the TBP-domain superfamily.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
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- Early Evolution of Transcription Systems and Divergence of Archaea and Bacteria.Frontiers in molecular biosciences · 2021Review
- Molecular determinants underlying functional innovations of TBP and their impact on transcription initiation.Nature communications · 2020Article
- Mosaic origin of the eukaryotic kinetochore.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Generation of a Small Library of Natural Products Designed to Cover Chemical Space Inexpensively.Pharmaceutical frontiers · 2019Article
- The cutting edge of archaeal transcription.Emerging topics in life sciences · 2018Article
- Displacement of the transcription factor B reader domain during transcription initiation.Nucleic acids research · 2018Article
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- A model for genesis of transcription systems.Transcription · 2016Article
- Analyses of in vivo interactions between transcription factors and the archaeal RNA polymerase.Methods (San Diego, Calif.) · 2015Article
- The case for an early biological origin of DNA.Journal of molecular evolution · 2014Article
- Crystal structure of RNase H3-substrate complex reveals parallel evolution of RNA/DNA hybrid recognition.Nucleic acids research · 2014Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
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.
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