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Elongation factor G with effector loop from elongation factor Tu is inactive in translocation
Alexander Kolesnikov1, Anatoly Gudkov
1Institute of Protein Research, Russian Academy of Sciences, 142290, Moscow Region, Pushchino, Russia.
FEBS Letters
|March 21, 2002
Summary
The effector loop of elongation factor G (EF-G) was swapped with that from elongation factor Tu (EF-Tu). This modification significantly reduced EF-G
Area of Science:
- Molecular Biology
- Protein Biosynthesis
- Structural Biology
Background:
- Elongation factors Tu (EF-Tu) and G (EF-G) are crucial for protein biosynthesis.
- Both factors bind GTP and belong to the G-protein superfamily, featuring an effector loop for target interaction.
Purpose of the Study:
- To investigate the functional interchangeability of effector loops between EF-Tu and EF-G.
- To determine the role of the effector loop in the distinct functions of EF-G.
Main Methods:
- Site-directed mutagenesis was used to replace the effector loop of EF-G with the corresponding loop from EF-Tu.
- GTPase activity assays were performed to assess the functionality of the modified EF-G.
Main Results:
- The modified EF-G, containing the EF-Tu effector loop, exhibited significantly reduced GTPase activity.
- The mutated factor failed to catalyze the translocation step in protein synthesis.
Conclusions:
- The effector loops of EF-Tu and EF-G are not functionally interchangeable.
- Distinct ribosome interactions necessitate specific structural features within the effector loops of these elongation factors.