Literature DB >> 12460561

Genetic perturbations of RNA reveal structure-based recognition in protein-RNA interaction.

Hyunsic Choi1, Sharee Otten, Jay Schneider, William H McClain.   

Abstract

Protein-RNA recognition is an essential foundation of cellular processes, yet much remains unknown about these important interactions. The recognition between aminoacyl-tRNA synthetases and their cognate tRNA substrates is highly specific and essential for cell viability, due to the necessity for accurate translation of the genetic code into protein sequences. We selected an active tRNA that is highly mutated in the recognition nucleotides of the acceptor stem region in the alanine system. The functional properties of this mutant and its secondary derivatives demonstrate that recognition cannot be reduced to isolated structural elements, but rather the amino acid acceptor stem is being recognized as a unit.

Entities:  

Mesh:

Substances:

Year:  2002        PMID: 12460561     DOI: 10.1016/s0022-2836(02)01098-7

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  3 in total

1.  Surprising contribution to aminoacylation and translation of non-Watson-Crick pairs in tRNA.

Authors:  William H McClain
Journal:  Proc Natl Acad Sci U S A       Date:  2006-03-14       Impact factor: 11.205

2.  Revisiting the operational RNA code for amino acids: Ensemble attributes and their implications.

Authors:  Shaul Shaul; Dror Berel; Yoav Benjamini; Dan Graur
Journal:  RNA       Date:  2009-12-01       Impact factor: 4.942

3.  Recognition of acceptor-stem structure of tRNA(Asp) by Escherichia coli aspartyl-tRNA synthetase.

Authors:  Hyunsic Choi; Kay Gabriel; Jay Schneider; Sharee Otten; William H McClain
Journal:  RNA       Date:  2003-04       Impact factor: 4.942

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.