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Scientific result | Molecular mechanisms | Structural biology | Simulation ＆ modelling
Using molecular dynamics simulation and NMR studies, I2BC researchers detail the mechanisms of restriction of BAF protein dynamics due to its phosphorylation. In particular, they describe the dynamic network of interactions, involving the phosphorylated residues pS4 and pT3, responsible for this conformational restriction.
The Barrier-to-Autointegration Factor (BAF protein) is a highly conserved protein that has the ability to bind to DNA and nuclear envelope proteins. Several studies suggest an important role for BAF in chromatin organization and genome integrity. Its localization and function are regulated by phosphorylation. Researchers of the team "Nuclear envelope, telomere and DNA repair" (B3S/I2BC) are interested in this protein and particularly in its interaction mechanisms with its protein partners (lamin, emerin) or nucleic partners. In a previous study (news of March 29, 2021 "Phosphorylation of BAF alters its dynamics and interaction with DNA but not its contacts with the nuclear envelope"), the researchers showed that mitotic phosphorylation of BAF rigidifies the structure of its N-terminal region, and leads to its dissociation from DNA but not to its binding to emerin and lamin proteins.
In a new study, published in the Journal of Molecular Biology, the team designed a molecular dynamics simulation protocol that allowed them to reveal the dynamic network of interactions that contribute to the conformational restriction of the N-terminal region of BAF.
In a new study, published in the Journal of Molecular Biology, the team designed a molecular dynamics simulation protocol that allowed them to reveal the dynamic network of interactions that contribute to the conformational restriction of the N-terminal region of BAF. The study shows that the conformation of the intrinsically disordered N-terminal region of BAF is highly adjustable, probably in connection with its various functions. This study also shows the contribution of numerical simulation in the context of structural biology for the study of the effect of post-translational modifications on the structure and dynamics of proteins.
To learn more, read the news published on the I2BC website in December 2022: "How Molecular Dynamics simulation and NMR show the effect of phosphorylation and pH on the conformational regulation of the intrinsically desordered N-terminal region of Barrier-to-Integration factor (BAF) at the atomic scale"
Agathe Marcelot, Sophie Zinn-Justin, Philippe Cuniasse. The Conformation of the Intrinsically Disordered N-Terminal Region of Barrier-to-Autointegration Factor (BAF) is Regulated by pH and Phosphorylation. | J. Mol. Bio., 2023, 43(2) https://doi.org/10.1016/j.jmb.2022.167888
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