Translation of a histone H3 tail as a model system for studying peptidyl-tRNA drop-off.

Authors :: Kang TJ
Suga H
Source :: FEBS letters [FEBS Lett] 2011 Jul 21; Vol. 585 (14), pp. 2269-74. Date of Electronic Publication: 2011 May 27.
Publication Year :: 2011
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.<br /> (Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)

Subjects :: Amino Acid Sequence
Codon
Histones genetics
Mass Spectrometry methods
Molecular Sequence Data
Molecular Structure
Peptide Chain Termination, Translational genetics
Peptide Fragments chemistry
Peptide Fragments genetics
Peptide Fragments metabolism
Histones chemistry
Histones metabolism
Protein Biosynthesis
RNA, Transfer, Amino Acyl metabolism

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