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Updated: Jul 11, 2025

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
Published on: October 8, 2015
Archaeal GPN-loop GTPases involve a lock-switch-rock mechanism for GTP hydrolysis
Lukas Korf1, Xing Ye2, Marian S Vogt1
1Department of Chemistry, Philipps University, Marburg, Germany.
Importance:
GPN-loop GTPases have been found to be crucial for eukaryotic RNA polymerase II assembly and nuclear trafficking. Despite their ubiquitous occurrence in eukaryotes and archaea, the mechanism by which these GTPases mediate their function is unknown. Our study on an archaeal representative from Sulfolobus acidocaldarius showed that these dimeric GTPases undergo large-scale conformational changes upon GTP hydrolysis, which can be summarized as a lock-switch-rock mechanism. The observed requirement of SaGPN for motility appears to be due to its large footprint on the archaeal proteome.
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