Click
here to close Hello! We notice that
you are using Internet Explorer, which is not supported by Echinobase
and may cause the site to display incorrectly. We suggest using a
current version of Chrome,
FireFox,
or Safari.
Protein Sci
2020 Jul 01;297:1687-1691. doi: 10.1002/pro.3868.
Show Gene links
Show Anatomy links
High affinity between CREBBP/p300 and NCOA evolved in vertebrates.
Karlsson E
,
Lindberg A
,
Andersson E
,
Jemth P
.
???displayArticle.abstract???
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. Blue‐green 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 (blue‐green) 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
Anthis,
Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm.
2013, Pubmed
Anthis,
Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm.
2013,
Pubmed
Christoffels,
Fugu genome analysis provides evidence for a whole-genome duplication early during the evolution of ray-finned fishes.
2004,
Pubmed
Demarest,
Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB-binding protein.
2004,
Pubmed
Demarest,
Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators.
2002,
Pubmed
Dogan,
Fast association and slow transitions in the interaction between two intrinsically disordered protein domains.
2012,
Pubmed
Goodman,
CBP/p300 in cell growth, transformation, and development.
2000,
Pubmed
Hultqvist,
Emergence and evolution of an interaction between intrinsically disordered proteins.
2017,
Pubmed
Jemth,
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins.
2018,
Pubmed
Karlsson,
A structurally heterogeneous transition state underlies coupled binding and folding of disordered proteins.
2019,
Pubmed
Kjaergaard,
Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP.
2010,
Pubmed
McLysaght,
Extensive genomic duplication during early chordate evolution.
2002,
Pubmed
Xu,
Review of the in vivo functions of the p160 steroid receptor coactivator family.
2003,
Pubmed
