Archaeal GPN-loop GTPases involve a lock-switch-rock mechanism for GTP hydrolysis.
- Resource Type
- Academic Journal
- Authors
- Korf L; Department of Chemistry, Philipps University, Marburg, Germany.; Ye X; University of Freiburg, Institute of Biology, Molecular Biology of Archaea, Freiburg, Germany.; Vogt MS; Department of Chemistry, Philipps University, Marburg, Germany.; Steinchen W; Department of Chemistry, Philipps University, Marburg, Germany.; Center for Synthetic Microbiology (SYNMIKRO), Karl-von-Frisch-Strasse, Marburg, Germany.; Watad M; Department of Chemistry, Philipps University, Marburg, Germany.; van der Does C; University of Freiburg, Institute of Biology, Molecular Biology of Archaea, Freiburg, Germany.; Tourte M; University of Freiburg, Institute of Biology, Molecular Biology of Archaea, Freiburg, Germany.; Sivabalasarma S; University of Freiburg, Institute of Biology, Molecular Biology of Archaea, Freiburg, Germany.; Spemann Graduate School of Biology and Medicine, University of Freiburg, Freiburg, Germany.; Albers S-V; University of Freiburg, Institute of Biology, Molecular Biology of Archaea, Freiburg, Germany.; Essen L-O; Department of Chemistry, Philipps University, Marburg, Germany.
- Source
- Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 101519231 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2150-7511 (Electronic) NLM ISO Abbreviation: mBio Subsets: MEDLINE
- Subject
- Language
- English
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 Sa GPN for motility appears to be due to its large footprint on the archaeal proteome.