About: The protonation state of an evolutionarily conserved histidine modulates domainswapping stability of FoxP1

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About: The protonation state of an evolutionarily conserved histidine modulates domainswapping stability of FoxP1 Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The protonation state of an evolutionarily conserved histidine modulates domainswapping stability of FoxP1
Creator	Babul, Jorge Coñuecar, Ricardo Medina, Exequiel Ramírez-Sarmiento, César Villalobos, Pablo
Source	PMC
abstract	Forkhead box P (FoxP) proteins are members of the versatile Fox transcription factors, which control the timing and expression of multiple genes for eukaryotic cell homeostasis. Compared to other Fox proteins, they can form domain-swapped dimers through their DNA-binding –forkhead– domains, enabling spatial reorganization of distant chromosome elements by tethering two DNA molecules together. Yet, domain swapping stability and DNA binding affinity varies between different FoxP proteins. Experimental evidence suggests that the protonation state of a histidine residue conserved in all Fox proteins is responsible for pH-dependent modulation of these interactions. Here, we explore the consequences of the protonation state of another histidine (H59), only conserved within FoxM/O/P subfamilies, on folding and dimerization of the forkhead domain of human FoxP1. Dimer dissociation kinetics and equilibrium unfolding experiments demonstrate that protonation of H59 leads to destabilization of the domain-swapped dimer due to an increase in free energy difference between the monomeric and transition states. This pH–dependence is abolished when H59 is mutated to alanine. Furthermore, anisotropy measurements and molecular dynamics evidence that H59 has a direct impact in the local stability of helix H3. Altogether, our results highlight the relevance of H59 in domain swapping and folding stability of FoxP1.
has issue date	2019-04-01(xsd:dateTime)
bibo:doi	10.1038/s41598-019-41819-5
bibo:pmid	30931977
has license	cc-by
sha1sum (hex)	b6ffbfa9a7a61fc231df2d34690da73211365c18
schema:url	https://doi.org/10.1038/s41598-019-41819-5
resource representing a document's title	The protonation state of an evolutionarily conserved histidine modulates domainswapping stability of FoxP1
has PubMed Central identifier	PMC6443806
has PubMed identifier	30931977
schema:publication	Sci Rep
resource representing a document's body	covid:b6ffbfa9a7a61fc231df2d34690da73211365c18#body_text
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