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<p>The functional importance of the methylation of histidine 73 (H73) in actin remains unclear. Focusing on cytoplasmic <i>β</i>-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 <i>β</i>-actin plasticity and integrates environmental cues.</p>

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Histidine 73 methylation coordinates β-actin plasticity in response to key environmental factors

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年3月7日

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  • Adrien Schahl,
  • Louis Lagardère,
  • Brandon Walker,
  • Pengyu Ren,
  • Hugo Wioland,
  • Maya Ballet,
  • Antoine Jégou,
  • Matthieu Chavent,
  • Jean-Philip Piquemal

摘要

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.