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Phenylalanyl-tRNA synthetase

Authors Chakraborty S, Banerjee R

Received 30 July 2015

Accepted for publication 7 November 2015

Published 8 June 2016 Volume 2016:6 Pages 25—38

DOI https://doi.org/10.2147/RRBC.S83482

Checked for plagiarism Yes

Review by Single-blind

Peer reviewers approved by Dr Supriya Swarnkar

Peer reviewer comments 3

Editor who approved publication: Professor Nikolay Dokholyan

Shruti Chakraborty, Rajat Banerjee

Department of Biotechnology, University of Calcutta, Kolkata, West Bengal, India

Abstract: Phenylalalnyl-tRNA synthetase (PheRS), a member of class II aminoacyl-tRNA synthetases, catalyzes the synthesis of phenylalanyl-tRNAPhe (Phe-tRNAPhe). Hence, like other aminoacyl-tRNA synthetases, PheRS also plays a crucial role in the cellular translation process. Structural characterization demonstrates remarkable architectural diversity ranging from monomer to hetero-oligomer. Heterotetrameric PheRS contains an editing domain to proofread misincorporation of non-cognate amino acids. However, editing activity is absent in monomeric PheRS. PheRS has also shown some noncanonical functions, such as DNA binding properties, suggesting its involvement in complex regulatory pathways. Engineered mutants with relaxed substrate specificities of PheRS can be a promising tool for chemical and synthetic biology. Because of substantial structural variations among species due to evolutionary divergence, PheRS may be validated as a novel drug target. Human PheRS gene mutations have recently been implicated in several neurological disorders prompting structure-function studies to elucidate the molecular role of PheRS in such pathologies. In this review on PheRS, we will briefly cover all of the aforementioned aspects and our current understanding about the enzyme.

Keywords: PheRS, structural organization, editing, disease, unnatural amino acid, drug targeting

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