title: Translation of a histone H3 tail as a model system for studying peptidyl-tRNA drop-off.
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.
authors.affiliation: Department of Chemical and Biochemical Engineering, Dongguk University-Seoul, Seoul, South Korea. taekkang@dongguk.edu
authors.forename: Taek Jin
authors.initials: TJ
authors.lastname: Kang
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Suga
mesh_terms: D000595:Amino Acid Sequence; D003062:Codon; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010443:Peptide Chain Termination, Translational / Q000235:genetics; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014176:Protein Biosynthesis; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*
chemical_list: D003062:Codon; D006657:Histones; D010446:Peptide Fragments; D012346:RNA, Transfer, Amino Acyl; C019037:tRNA, peptidyl-