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