Sequential Unfolding Mechanisms of Monomeric Caspases.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
20 06 2023
20 06 2023
Historique:
medline:
21
6
2023
pubmed:
20
6
2023
entrez:
20
6
2023
Statut:
ppublish
Résumé
Caspases are evolutionarily conserved cysteinyl proteases that are integral in cell development and apoptosis. All apoptotic caspases evolved from a common ancestor into two distinct subfamilies with either monomeric (initiators) or dimeric (effectors) oligomeric states. The regulation of apoptosis is influenced by the activation mechanism of the two subfamilies, but the evolution of the well-conserved caspase-hemoglobinase fold into the two subfamilies is not well understood. We examined the folding landscape of monomeric caspases from two coral species over a broad pH range of 3-10.5. On an evolutionary timescale, the two coral caspases diverged from each other approximately 300 million years ago, and they diverged from human caspases about 600 million years ago. Our results indicate that both proteins have overall high stability, ∼15 kcal mol
Identifiants
pubmed: 37337671
doi: 10.1021/acs.biochem.3c00004
pmc: PMC10286309
doi:
Substances chimiques
Caspases
EC 3.4.22.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
1878-1889Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM127654
Pays : United States
Commentaires et corrections
Type : UpdateOf
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