Cargando…
Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA Deacylase
D-aminoacyl-tRNA deacylase (DTD) removes D-amino acids mischarged on tRNAs and is thus implicated in enforcing homochirality in proteins. Previously, we proposed that selective capture of D-aminoacyl-tRNA by DTD’s invariant, cross-subunit Gly-cisPro motif forms the mechanistic basis for its enantios...
Autores principales: | Routh, Satya Brata, Pawar, Komal Ishwar, Ahmad, Sadeem, Singh, Swati, Suma, Katta, Kumar, Mantu, Kuncha, Santosh Kumar, Yadav, Kranthikumar, Kruparani, Shobha P, Sankaranarayanan, Rajan |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4880308/ https://www.ncbi.nlm.nih.gov/pubmed/27224426 http://dx.doi.org/10.1371/journal.pbio.1002465 |
Ejemplares similares
-
Role of D-aminoacyl-tRNA deacylase beyond chiral proofreading as a cellular defense against glycine mischarging by AlaRS
por: Pawar, Komal Ishwar, et al.
Publicado: (2017) -
A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia
por: Kuncha, Santosh Kumar, et al.
Publicado: (2018) -
Specificity and catalysis hardwired at the RNA–protein interface in a translational proofreading enzyme
por: Ahmad, Sadeem, et al.
Publicado: (2015) -
Kinetic Proofreading at Single Molecular Level: Aminoacylation of tRNA(Ile) and the Role of Water as an Editor
por: Santra, Mantu, et al.
Publicado: (2013) -
Design principles and functional basis of enantioselectivity of alanyl-tRNA synthetase and a chiral proofreader during protein biosynthesis
por: Sivakumar, Koushick, et al.
Publicado: (2023)