An elongation factor turn-on
Article Abstract:
The elongation factors EF-Tu and EF-G in bacteria and EF-1-alpha and EF-2 in other organisms catalyze the elongation of amino acid chains and regulate protein synthesis. They are similar to G-proteins and switch from inactive to active states by binding GTP and GDP. EF-G catalyzes ribosomal conversion from the pre- to post-translational state, while EF-Tu catalyzes the reverse reaction. The crystal structures of GDP-bound and free EF-G reveal that the tRNA part of the ternary complex, aminoacyl-tRNA.EF-Tu.GTP, and the domains 3 to 5 of EF-G are similar.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
Article Abstract:
Guanosine triphosphatase (GTP) analogues promote translocation, and GTP hydrolysis accelerates translocation in both single and multiple turnover. Elongation factor G (EF-G)-dependent GTP hydrolysis has been proven to precede and facilitate the rearrangement of the ribosome that leads to translocation. By using the free energy resulting from GTP hydrolysis to translocation, EF-G serves as a motor protein to drive the directional movement of tRNAs and mRNAs on the ribosome.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Visualization of elongation factor Tu on the Escherichia coli ribosome
Article Abstract:
Protein synthesis relies on the delivery of specific amino acids to the translating ribosome. The elongation factor Tu is a catalyst for the binding of aminoacyl-transfer RNA (tRNA) to the ribosome, and together with the aminoacyl-tRNA and GTP form a stable ternary complex. Electron microscopy shows the 70S Escherichia coli ribosome with the ternary complex locked into the A site by the antibiotic kirromycin.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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