Abstract
Aminoacyl-tRNA synthetases often rely on a proofreading mechanism to clear mischarging errors before they can be incorporated into newly synthesized proteins. Leucyl-tRNA synthetase (LeuRS) houses a hydrolytic editing pocket in a domain that is distinct from its aminoacylation domain. Mischarged amino acids are transiently translocated ∼30 Å between active sites for editing by an unknown tRNA-dependent mechanism. A glycine within a flexible β-strand that links the aminoacylation and editing domains of LeuRS was determined to be important to tRNA translocation. The translocation-defective mutation also demonstrated that the editing site screens both correctly and incorrectly charged tRNAs prior to product release.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3443-3447 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 583 |
| Issue number | 21 |
| DOIs | |
| State | Published - Nov 3 2009 |
Keywords
- Amino acid editing
- Fidelity
- Protein synthesis
- Translocation
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Mascarenhas, A. P., & Martinis, S. A. (2009). A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase. FEBS Letters, 583(21), 3443-3447. https://doi.org/10.1016/j.febslet.2009.09.039