High affinity between CREBBP/p300 and NCOA evolved in vertebrates.
ACTR
CBP
CID
CREBBP
NCBD
echinoderm
intrinsically disordered protein
p300
protein evolution
protein-protein interaction
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
07 2020
07 2020
Historique:
received:
13
02
2020
revised:
04
04
2020
accepted:
05
04
2020
pubmed:
25
4
2020
medline:
16
1
2021
entrez:
25
4
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32329110
doi: 10.1002/pro.3868
pmc: PMC7314397
doi:
Substances chimiques
Nuclear Receptor Coactivators
0
p300-CBP Transcription Factors
EC 2.3.1.48
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1687-1691Informations de copyright
© 2020 The Authors. Protein Science published by Wiley Periodicals, Inc. on behalf of The Protein Society.
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