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June 17, 2026The Journal of Biochemistry

Structure and biochemical analyses suggest that PrkA/YeaG protein of Thermus thermophilus functions as a putative molecular chaperone

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Authors

MTMasayuki ToriiRKR KannoAMAkira Mizoguchi

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Overview

Biochemical analyses reveal chaperone-like activities in TpkB, a putative member of the AAA+ superfamily.

Key Points

  • This study aims to elucidate the structural and functional roles of the PrkA/YeaG homologue TpkB in Thermus thermophilus.
  • Determined the structures of TpkB using cryo-electron microscopy in both apo and AMPPNP-bound forms.
  • Conducted structural and gene neighborhood analyses to explore functional links with vWA domain proteins.
  • Performed biochemical assays to evaluate ATPase and chaperone-like activities of TpkB.
  • TpkB exhibits structural features consistent with AAA+ superfamily proteins, including hexameric ring architecture.
  • Demonstrated ATPase activity and chaperone-like function while lacking detectable protein kinase activity.
  • Establishes TpkB as a potential chaperone, expanding the understanding of the PrkA/YeaG family.

Cite This Study

Torii et al. (2026) studied this question.

synapsesocial.com/papers/6a323b4cd50b63ecad205fa0https://doi.org/10.1093/jb/mvag041
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