The role of initiator tRNA I met in fidelity of initiation of protein synthesis
Document Type
Article
Publication Date
1-1-2011
Abstract
The proper arrangement of amino acids in a protein determines its proper function, which is vital for the cellular metabolism. This indicates that the process of peptide bond formation requires high fidelity. One of the most important processes for this fidelity is kinetic proofreading. As biochemical experiments suggest that kinetic proofreading plays a major role in ensuring the fidelity of protein synthesis, it is not certain whether or not a misacylated tRNA would be corrected by kinetic proofreading during the peptide bond formation. Using 2-layered ONIOM (QM/MM) computational calculations, we studied the behavior of misacylated tRNAs and compared the results with these for cognate aminoacyl-tRNAs during the process of peptide bond formation to investigate the effect of nonnative amino acids on tRNAs. The difference between the behavior of initiator tRNA i met compared to the one for the elongator tRNAs indicates that only the initiator tRNA i met specifies the amino acid side chain. Copyright © Taylor and Francis Group, LLC.
Keywords
ONIOM, peptide bond formation, ribosome, tRNA, amino acid, aminoacyl transfer RNA, transfer RNA, methionine transfer RNA, protein, article, electron transport, molecular mechanics, protein binding, protein function, protein structure, protein synthesis, quantum mechanics, RNA structure, chemistry, genetics, metabolism, RNA translation, X ray crystallography, Crystallography, X-Ray, Peptide Chain Initiation, Translational, Protein Biosynthesis, Proteins, Ribosomes, RNA, Transfer, Met RNA, Transfer, Met
Divisions
CHEMISTRY
Publication Title
Nucleosides, Nucleotides and Nucleic Acids
Volume
30
Issue
9
Additional Information
Department of Chemistry, Faculty of Science Building, University of Malaya, 50603 Kuala Lumpur, MALAYSIA