Histidine 73 methylation coordinates β-actin plasticity in response to key environmental factors
Adrien Schahl,
Louis Lagardère,
Brandon Walker,
Pengyu Ren,
Hugo Wioland,
Maya Ballet,
Antoine Jégou,
Matthieu Chavent () and
Jean-Philip Piquemal ()
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Adrien Schahl: Université de Toulouse, CNRS
Louis Lagardère: Sorbonne Université, UMR 7616 CNRS
Brandon Walker: The University of Texas at Austin
Pengyu Ren: The University of Texas at Austin
Hugo Wioland: Université Paris Cité, CNRS
Maya Ballet: Université Paris Cité, CNRS
Antoine Jégou: Université Paris Cité, CNRS
Matthieu Chavent: Université de Toulouse, CNRS
Jean-Philip Piquemal: Sorbonne Université, UMR 7616 CNRS
Nature Communications, 2025, vol. 16, issue 1, 1-13
Abstract:
Abstract The functional importance of the methylation of histidine 73 (H73) in actin remains unclear. Focusing on cytoplasmic β-actin, present in all mammalian cells, we use molecular dynamics simulations with a polarizable force field and adaptive sampling to examine the effects of H73 methylation. Our results show that methylation enhances nucleotide binding cleft opening, alters allosteric pathways connecting subdomains 2 and 4 (SD2 and SD4) in G-actin, and affects backdoor openings and inorganic phosphate release in F-actin, as validated by biochemical assays. These effects depend on the nucleotide and ions interacting with the actin. Together, our findings reveal how H73 methylation regulates β-actin plasticity and integrates environmental cues.
Date: 2025
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57458-6
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DOI: 10.1038/s41467-025-57458-6
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