Dissecting the structural and functional consequences of the evolutionary proline-glycine deletion in the wing 1 region of the forkhead domain of human FoxP1.
DNA‐binding affinity
P subfamily
domain swapping
evolutionary mutations
forkhead DNA‐binding proteins
protein–protein interactions
stability
transcription factor
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
30 Jun 2024
30 Jun 2024
Historique:
revised:
06
06
2024
received:
08
04
2024
accepted:
07
06
2024
medline:
1
7
2024
pubmed:
1
7
2024
entrez:
1
7
2024
Statut:
aheadofprint
Résumé
The human FoxP transcription factors dimerize via three-dimensional domain swapping, a unique feature among the human Fox family, as result of evolutionary sequence adaptations in the forkhead domain. This is the case for the conserved glycine and proline residues in the wing 1 region, which are absent in FoxP proteins but present in most of the Fox family. In this work, we engineered both glycine (G) and proline-glycine (PG) insertion mutants to evaluate the deletion events in FoxP proteins in their dimerization, stability, flexibility, and DNA-binding ability. We show that the PG insertion only increases protein stability, whereas the single glycine insertion decreases the association rate and protein stability and promotes affinity to the DNA ligand.
Identifiants
pubmed: 38946055
doi: 10.1002/1873-3468.14972
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Fondo Nacional de Desarrollo Científico y Tecnológico
ID : 11200729
Organisme : Fondo Nacional de Desarrollo Científico y Tecnológico
ID : 1170701
Organisme : Fondo Nacional de Desarrollo Científico y Tecnológico
ID : 1201684
Organisme : Fondo Nacional de Desarrollo Científico y Tecnológico
ID : 21181705
Organisme : Fondo Nacional de Desarrollo Científico y Tecnológico
ID : 3240319
Organisme : Agencia Nacional de Investigación y Desarrollo
ID : Millennium Science Initiative Program (ICN17_022)
Informations de copyright
© 2024 Federation of European Biochemical Societies.
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