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Protein Sci
2020 Jul 01;297:1687-1691. doi: 10.1002/pro.3868.
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High affinity between CREBBP/p300 and NCOA evolved in vertebrates.
Karlsson E
,
Lindberg A
,
Andersson E
,
Jemth P
.
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The interaction between the transcriptional coactivators CREBBP/p300 and NCOA is governed by two intrinsically disordered domains called NCBD and CID, respectively. The CID domain emerged within the NCOA protein in deuterostome animals (including vertebrates) after their split from the protostomes (molluscs, worms, and arthropods). However, it has not been clear at which point a high affinity interaction evolved within the deuterostome clade and whether all present-day deuterostome animals have a high affinity NCBD:CID interaction. We have here expressed and measured affinity for NCBD and CID domains from animal species representing different evolutionary branches of the deuterostome tree. While all vertebrate species have high-affinity NCBD:CID interactions we found that the interaction in the echinoderm purple sea urchin is of similar affinity as that of the proposed ancestral domains. Our findings demonstrate that the high-affinity NCBD:CID interaction likely evolved in the vertebrate branch and question whether the interaction between CREBBP/p300 and NCOA is essential in nonvertebrate deuterostomes. The data provide an example of evolution of transcriptional regulation through protein-domain based inventions.
FIGURE 1. NCBD and CID: evolution, structure, and affinities. (a) A schematic phylogenetic tree showing the evolutionary relationship between extant species along with binding affinities of NCBD:CID complexes determined by ITC. Blueâgreen color denotes the evolutionary tree for NCBD and olive denotes the evolution of CID. The schematic animals were downloaded from http://phylopic.org. (b) Solution structure of the human complex consisting of NCBD from CREBBP (blueâgreen) and CID from NCOA3/ACTR (olive; PDB entry 6ES7). (c) NCBD (top) and CID (bottom) sequences from four species. Two CID paralogues were identified in Petromyzon marinus. The sequence alignments were performed using PRALINE and the colour coding denotes residue type. (d) Example ITC thermograms for the human (Homo sapiens) complex (left) and purple sea urchin (S. purpuratus) complex (right). (e) The binding affinities of the NCBD:CID complexes in different animals. Each experiment was performed at least twice and the error bars denote the SEM for replicate or triplicate experiments
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