A New TRNA-assisted Mechanism Of Post-transfer Editing By Aminoacyl-tRNA Synthetases | 63603
ISSN: 2155-952X

Journal of Biotechnology & Biomaterials
Open Access

Like us on:

Our Group organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations
700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)
Recommended Conferences

6th International Conference on Vaccines and Immunology

Geneva, Switzerland

3rd European Congress on Virology

Geneva, Switzerland
Google Scholar citation report
Citations : 1600

Journal of Biotechnology & Biomaterials received 1600 citations as per Google Scholar report

Indexed In
  • Index Copernicus
  • Google Scholar
  • Sherpa Romeo
  • Open J Gate
  • Genamics JournalSeek
  • Academic Keys
  • ResearchBible
  • China National Knowledge Infrastructure (CNKI)
  • Access to Global Online Research in Agriculture (AGORA)
  • Electronic Journals Library
  • RefSeek
  • Hamdard University
  • OCLC- WorldCat
  • SWB online catalog
  • Virtual Library of Biology (vifabio)
  • Publons
  • Geneva Foundation for Medical Education and Research
  • Euro Pub
Share This Page

A new tRNA-assisted mechanism of post-transfer editing by aminoacyl-tRNA synthetases

Joint Event on 15th World Congress on Biotechnology And Biotech Industries Meet and 2nd International Conference on Enzymology and Molecular Biology

Mykhaylo Tukalo

National Academy of Sciences of Ukraine, Ukraine

Posters & Accepted Abstracts: J Biotechnol Biomater

DOI: 10.4172/2155-952X.C1.071

Statement of the Problem: Aminoacyl-tRNA synthetases (aaRSs) maintain fidelity during protein synthesis by attaching amino acids to their cognate tRNAs. For many aaRSs, the required level of amino-acid specificity is achieved either by specific hydrolysis of misactivated aminoacyl-adenylate intermediate (pre-transfer editing) or by hydrolysis of the mischarged aminoacyl-tRNA (post-transfer editing). Both reactions are depend on a tRNA cofactor and required translocation to the editing site located in the separate domain. In this work we have studied molecular mechanisms of editing by synthetases from two different classes: Thermus thermophilus leucyl-tRNA synthetase (LeuRSTT) from class I and Enterococcus faecalis prolyl-tRNA synthetase (ProRSEF) from class II. Methodology & Theoretical Orientation: To investigate the mechanism of post-transfer editing of norvaline by LeuRSTT and alanine by ProRSEF, we used molecular modeling, molecular dynamic (MD) simulations, quantum mechanical (QM) calculations, site-directed mutagenesis of the enzymes and tRNA modification. The transition states of the reactions were identified. Findings: The results support a new tRNA-assisted mechanism of hydrolysis of misacylated tRNA which directly involves two water molecules. The most important functional element of this catalytic mechanism is the 2' or 3’-OH group of the terminal adenosine 76 of aminoacyl-tRNA, which forms an intra-molecular hydrogen bond with the carbonyl group of the misacylated residue. Bonding increases the electrophilic character of the carbon atom and strongly facilitates the subsequent nucleophilic attack by water molecule. Conclusion & Significance: Class I LeuRS and class II ProRS with a different architecture of editing site have both tRNA-assisted mechanism of post-transfer editing in which free 2’ or 3’-OH group of the substrate plays a key role in hydrolysis by forming an intramolecular hydrogen bond with the substrate amino-acid carbonyl group. Proposed editing mechanism is significantly different from those described in the literature for class-I and class-II aaRSs.

Email: [email protected]