Nature Communications (Aug 2021)

CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin

  • Yanyan Zhao,
  • Michael F. Schmid,
  • Judith Frydman,
  • Wah Chiu

DOI
https://doi.org/10.1038/s41467-021-25099-0
Journal volume & issue
Vol. 12, no. 1
pp. 1 – 10

Abstract

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The mechanism by which chaperonins coordinate ATP utilization in their multiple subunits remains unclear. Here, the authors employ an approach that uses cryo-EM single particle analysis to track the number and distribution of nucleotides bound to each subunit in the homo-oligomeric MmCpn archaeal chaperonin complex and observe that ATP binds in a statistically random manner to MmCpn both within a ring and across the rings, which shows that there is no cooperativity in ATP binding to archaeal group II chaperonins under the conditions used in this study.