Abstract
We found that the synthesis of histone H3 N-terminal peptide (tail) in a reconstituted protein synthesis system yielded fragmented peptides along with the full-length product. With the combined use of MALDI-TOF analysis and peptidyl-tRNA hydrolase cleavage of the Flag tagged product species, we concluded that the fragments were generated by peptidyl-tRNA drop-off at specific sites and subsequent translation continuation. Using the histone H3 tail we also found that peptidyl-tRNA drop-off is strongly correlated with the amino acid context. We envision that the system described here would be useful as a model system for studying peptidyl-tRNA drop-off events.
Original language | English |
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Pages (from-to) | 2269-2274 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 585 |
Issue number | 14 |
DOIs | |
State | Published - 21 Jul 2011 |
Keywords
- Peptidyl-tRNA drop-off
- Peptidyl-tRNA hydrolase
- Translation