title: Peptidyl-tRNA hydrolase and its critical role in protein biosynthesis.
abstract: 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.
authors.affiliation: Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
authors.forename: Gautam
authors.initials: G
authors.lastname: Das
authors.affiliation: Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
authors.forename: Umesh
authors.initials: U
authors.lastname: Varshney
mesh_terms: D002265:Carboxylic Ester Hydrolases / Q000235:genetics / Q000502:physiology*; D014176:Protein Biosynthesis; D012358:RNA, Transfer, Met / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D012358:RNA, Transfer, Met; C089238:fMet-tRNA(fMet); D002265:Carboxylic Ester Hydrolases; C019674:aminoacyl-tRNA hydrolase