Archaeal GPN-loop GTPases involve a lock-switch-rock mechanism for GTP hydrolysis

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 showed...

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Bibliographic Details
Published in:mBio 2023-12, Vol.14 (6), p.e0085923
Main Authors: Korf, Lukas, Ye, Xing, Vogt, Marian S, Steinchen, Wieland, Watad, Mohamed, van der Does, Chris, Tourte, Maxime, Sivabalasarma, Shamphavi, Albers, Sonja-Verena, Essen, Lars-Oliver
Format: Article
Language:English
Subjects:
allostery
GPN-loop
GTPase
Research Article
RNA polymerase II
Structural Biology
sulfolobus
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Summary: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 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 GPN for motility appears to be due to its large footprint on the archaeal proteome.
ISSN:2150-7511
2150-7511
DOI:10.1128/mbio.00859-23