תמונות העטיפה

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

Three GPN-loop GTPases, GPN1–GPN3, are central to the maturation and trafficking of eukaryotic RNA polymerase II. This GTPase family is widely represented in archaea but typically occurs as single paralogs. Structural analysis of the GTP- and GDP-bound states of the Sulfolobus acidocaldarius GPN enz...

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Autoren: 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,
פורמט: Artikel
שפה:אנגלית
יצא לאור: Philipps-Universität Marburg 2023
נושאים:
allostery
RNA polymerase II
GPN-loop
Chemie
GTPase
sulfolobus
Chemistry & allied sciences
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סיכום:Three GPN-loop GTPases, GPN1–GPN3, are central to the maturation and trafficking of eukaryotic RNA polymerase II. This GTPase family is widely represented in archaea but typically occurs as single paralogs. Structural analysis of the GTP- and GDP-bound states of the Sulfolobus acidocaldarius GPN enzyme (SaGPN) showed that this central GPN-loop GTPase adopts two distinct quaternary structures. In the GTP-bound form, the γ-phosphate induces a closed dimeric arrangement by interacting with the GPN region that is relaxed upon hydrolysis to GDP. Consequently, a rocking-like motion of the two protomers causes a major allosteric structural change toward the roof-like helices. Using a lock-switch-rock mechanism, homo- and heterodimeric GPN-like GTPases are locked in the GTP-bound state and undergo large conformational changes upon GTP hydrolysis. A ΔsaGPN strain of S. acidocaldarius was characterized by impaired motility and major changes in the proteome underscoring its functional relevance for S. acidocaldarius in vivo.
תאור פריט:Gefördert durch den Open-Access-Publikationsfonds der UB Marburg.
תיאור פיזי:22 Seiten
DOI:10.1128/mbio.00859-23

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