title: Evolutionary history of the TBP-domain superfamily.
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.
authors: Department of Botany, Stockholm University, 106 91 Stockholm, Sweden.
authors: Björn
authors: B
authors: Brindefalk
authors: Benoit H
authors: BH
authors: Dessailly
authors: Corin
authors: C
authors: Yeats
authors: Christine
authors: C
authors: Orengo
authors: Finn
authors: F
authors: Werner
authors: Anthony M
authors: AM
authors: Poole
mesh_terms: D000818:Animals; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics*; D016000:Cluster Analysis; D045647:DNA Glycosylases / Q000737:chemistry / Q000235:genetics*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics; D019143:Evolution, Molecular; D006801:Humans; D008957:Models, Genetic; D008958:Models, Molecular; D010802:Phylogeny; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary / Q000235:genetics; D012260:Ribonucleases / Q000737:chemistry / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D040681:Structural Homology, Protein; D035181:TATA-Box Binding Protein / Q000737:chemistry / Q000235:genetics*
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D035181:TATA-Box Binding Protein; D012260:Ribonucleases; C117079:ribonuclease HIII; D045647:DNA Glycosylases
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