Literature DB >> 17447878

Interaction of aminoacyl-tRNA synthetases with tRNA: general principles and distinguishing characteristics of the high-molecular-weight substrate recognition.

I A Vasil'eva1, N A Moor.   

Abstract

This review summarizes results of numerous (mainly functional) studies that have been accumulated over recent years on the problem of tRNA recognition by aminoacyl-tRNA synthetases. Development and employment of approaches that use synthetic mutant and chimeric tRNAs have demonstrated general principles underlying highly specific interaction in different systems. The specificity of interaction is determined by a certain number of nucleotides and structural elements of tRNA (constituting the set of recognition elements or specificity determinants), which are characteristic of each pair. Crystallographic structures available for many systems provide the details of the molecular basis of selective interaction. Diversity and identity of biochemical functions of the recognition elements make substantial contribution to the specificity of such interactions.

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Year:  2007        PMID: 17447878     DOI: 10.1134/s0006297907030029

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  6 in total

1.  Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerization.

Authors:  Masahiro Naganuma; Shun-ichi Sekine; Ryuya Fukunaga; Shigeyuki Yokoyama
Journal:  Proc Natl Acad Sci U S A       Date:  2009-05-07       Impact factor: 11.205

Review 2.  Emergence and evolution.

Authors:  Tammy J Bullwinkle; Michael Ibba
Journal:  Top Curr Chem       Date:  2014

3.  Expanding the amino acid repertoire of ribosomal polypeptide synthesis via the artificial division of codon boxes.

Authors:  Yoshihiko Iwane; Azusa Hitomi; Hiroshi Murakami; Takayuki Katoh; Yuki Goto; Hiroaki Suga
Journal:  Nat Chem       Date:  2016-02-01       Impact factor: 24.427

4.  Structural phylogenomics retrodicts the origin of the genetic code and uncovers the evolutionary impact of protein flexibility.

Authors:  Gustavo Caetano-Anollés; Minglei Wang; Derek Caetano-Anollés
Journal:  PLoS One       Date:  2013-08-21       Impact factor: 3.240

5.  A metabolic prototype for eliminating tryptophan from the genetic code.

Authors:  V Pezo; D Louis; V Guérineau; J-P Le Caer; L Gaillon; R Mutzel; P Marlière
Journal:  Sci Rep       Date:  2013       Impact factor: 4.379

6.  Pyrrolysyl-tRNA synthetase-tRNA(Pyl) structure reveals the molecular basis of orthogonality.

Authors:  Kayo Nozawa; Patrick O'Donoghue; Sarath Gundllapalli; Yuhei Araiso; Ryuichiro Ishitani; Takuya Umehara; Dieter Söll; Osamu Nureki
Journal:  Nature       Date:  2008-12-31       Impact factor: 49.962

  6 in total

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