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Translation of a histone H3 tail as a model system for studying peptidyl‐tRNA drop‐off
Author(s) -
Kang Taek Jin,
Suga Hiroaki
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.05.051
Subject(s) - transfer rna , chemistry , translation (biology) , histone h3 , histone , biochemistry , cleavage (geology) , biology , rna , messenger rna , dna , paleontology , fracture (geology) , gene
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.