January 13, 2023
Journal Article

Cryo-EM structure of the diapause chaperone Artemin


The protein artemin constitutes over 10% of all protein in Artemia cysts during diapause and acts as both a RNA and protein chaperone. However, its mechanistic details remain elusive since no high-resolution structure of artemin exists. Here we report the full-length structure of artemin at 2.12 Å resolution. The cryo-EM map contains density for an intramolecular disulfide bond between Cys22-Cys61 and resolves the entire C-terminus extending into the core of the assembled protein cage. We also provide data supporting the role of C-terminal helix F towards stabilizing the dimer form that is believed to be important for its chaperoning activity. We were able to destabilize this effect by placing a tag at the C-terminus to fully pack the internal cavity and cause limited steric hindrance.

Published: January 13, 2023


Parvate A.D., S.M. Powell, J.T. Brookreson, T.H. Moser, I.V. Novikova, M. Zhou, and J.E. Evans. 2022. Cryo-EM structure of the diapause chaperone Artemin. Frontiers in Molecular Biosciences 9. PNNL-SA-170053. doi:10.3389/fmolb.2022.998562