Peptidyl-tRNA hydrolase and its critical role in protein biosynthesis

Microbiology. 2006 Aug;152(Pt 8):2191-5. doi: 10.1099/mic.0.29024-0.


Peptidyl-tRNA hydrolase (Pth) releases tRNA from peptidyl-tRNA by cleaving the ester bond between the peptide and the tRNA. Genetic analyses using Escherichia coli harbouring temperature-sensitive Pth have identified a number of translation factors involved in peptidyl-tRNA release. Accumulation of peptidyl-tRNA in the cells leads to depletion of aminoacyl-tRNA pools and halts protein biosynthesis. Thus, it is vital for cells to maintain Pth activity to deal with the pollution of peptidyl-tRNAs generated during the initiation, elongation and termination steps of protein biosynthesis. Interestingly, while eubacteria possess a single class of peptidyl-tRNA hydrolase, eukaryotes possess several such activities, making Pth a potential drug target to control eubacterial infections. This review discusses the aspects of Pth that relate to its history and biochemistry and its physiological connections with various cellular factors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / physiology*
  • Protein Biosynthesis*
  • RNA, Transfer, Met / metabolism
  • Substrate Specificity


  • RNA, Transfer, Met
  • fMet-tRNA(fMet)
  • Carboxylic Ester Hydrolases
  • aminoacyl-tRNA hydrolase