Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
Identification of two structural elements important for ribosome-dependent GTPase activity of elongation factor 4 (EF4/LepA).
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EF4 has ribosome-dependent multiple turnover GTPase activity similar to EF-G, and the conserved histidine His81 is essential for this activity.
"successive removal of the C-terminus impairs ribosome-dependent multiple turnover GTPase activity of EF4, which for the full-length protein is very similar to EF-G"
Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome.
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Cryo-EM structure of EF4-GTP-ribosome complex at 3.8 A resolution reveals the GTPase activation mechanism.
"we present the cryo-EM reconstitution of the GTP form of EF4 bound to the ribosome with P and E site tRNAs at 3.8-Å resolution"
The membrane-bound GTPase Guf1 promotes mitochondrial protein synthesis under suboptimal conditions.
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Yeast Guf1 binds to mitochondrial ribosomes in a GTP-dependent manner and promotes mitochondrial protein synthesis. This study characterizes the yeast mitochondrial ortholog, not the chloroplastic paralog represented by A0A2U1PS28.
"It binds to mitochondrial ribosomes in a GTP-dependent manner"
Elongation factor 4 remodels the A-site tRNA on the ribosome.
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Crystal structure at 2.6 A shows EF-4 bound to the ribosome with tRNAs, revealing the C-terminal domain contacts with the A-site tRNA acceptor stem.
"we present the crystal structure at 2.6-Å resolution of the Thermus thermophilus 70S ribosome bound to EF-4 with a nonhydrolyzable GTP analog and A-, P-, and E-site tRNAs"