The Seryl-tRNA synthetase/tRNASer acceptor stem interface is mediated via a specific network of water molecules

2011 ◽  
Vol 412 (4) ◽  
pp. 532-536 ◽  
Author(s):  
André Eichert ◽  
Dominik Oberthuer ◽  
Christian Betzel ◽  
Reinhard Geßner ◽  
Volker A. Erdmann ◽  
...  
Keyword(s):  
Trna Synthetase ◽  
Water Molecules ◽  
Acceptor Stem

Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase

Nature ◽  
1991 ◽  
Vol 352 (6332) ◽  
pp. 258-260 ◽  
Author(s):  
Martina Jahn ◽  
M. John Rogers ◽  
Dieter Söll
Keyword(s):  
Trna Synthetase ◽  
E Coli ◽  
Acceptor Stem ◽  
Recognition Elements

scholarly journals Evolution of acceptor stem tRNA recognition by class II prolyl-tRNA synthetase

2008 ◽  
Vol 36 (8) ◽  
pp. 2514-2521 ◽  
Author(s):  
S. An ◽  
G. Barany ◽  
K. Musier-Forsyth
Keyword(s):  
Class Ii ◽  
Trna Synthetase ◽  
Trna Recognition ◽  
Acceptor Stem

Critical Role of the Acceptor Stem of tRNAsMet in their Aminoacylation by Escherichia coli Methionyl-tRNA Synthetase

1993 ◽  
Vol 229 (1) ◽  
pp. 26-36 ◽  
Author(s):  
Thierry Meinnel ◽  
Yves Mechulam ◽  
Christine Lazennec ◽  
Sylvain Blanquet ◽  
Guy Fayat
Keyword(s):  
Escherichia Coli ◽  
Critical Role ◽  
Trna Synthetase ◽  
Acceptor Stem ◽  
Methionyl Trna Synthetase

scholarly journals Specific atomic groups and RNA helix geometry in acceptor stem recognition by a tRNA synthetase

1997 ◽  
Vol 94 (19) ◽  
pp. 10150-10154 ◽  
Author(s):  
P. J. Beuning ◽  
F. Yang ◽  
P. Schimmel ◽  
K. Musier-Forsyth
Keyword(s):  
Trna Synthetase ◽  
Acceptor Stem ◽  
Helix Geometry

scholarly journals The role of nucleotides in position 1 and 72 of the tRNATyr acceptor stem in aminoacylation by bovine tyrosyl-tRNA synthetase

2002 ◽  
Vol 18 (1) ◽  
pp. 71-75
Author(s):  
V. G. Naidenov ◽  
M. I. Vudmaska ◽  
G. Kh. Matsuka
Keyword(s):  
Trna Synthetase ◽  
Acceptor Stem

Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase

Biochimie ◽  
1993 ◽  
Vol 75 (12) ◽  
pp. 1041-1049 ◽  
Author(s):  
D.J. Wright ◽  
S.A. Martinis ◽  
M. Jahn ◽  
D. Söll ◽  
P. Schimmel
Keyword(s):  
Trna Synthetase ◽  
Acceptor Stem ◽  
Rna Hairpin ◽  
Helix Interactions

scholarly journals Human trans-editing enzyme displays tRNA acceptor-stem specificity and relaxed amino acid selectivity

2020 ◽  
Vol 295 (48) ◽  
pp. 16180-16190
Author(s):  
Oscar Vargas-Rodriguez ◽  
Marina Bakhtina ◽  
Daniel McGowan ◽  
Jawad Abid ◽  
Yuki Goto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Homo Sapiens ◽  
Strong Dependence ◽  
Trna Synthetase ◽  
Substrate Selection ◽  
Acceptor Stem ◽  
Bacterial Enzyme ◽  
Editing Domain ◽  
Exclusion Mechanism ◽  
Trna Acceptor

Accurate translation of genetic information into proteins is vital for cell sustainability. ProXp-ala prevents proteome-wide Pro-to-Ala mutations by hydrolyzing misacylated Ala-tRNAPro, which is synthesized by prolyl-tRNA synthetase. Bacterial ProXp-ala was previously shown to combine a size-based exclusion mechanism with conformational and chemical selection for the recognition of the alanyl moiety, whereas tRNAPro is selected via recognition of tRNA acceptor-stem elements G72 and A73. The identity of these critical bases changed during evolution with eukaryotic cytosolic tRNAPro possessing a cytosine at the corresponding positions. The mechanism by which eukaryotic ProXp-ala adapted to these changes remains unknown. In this work, recognition of the aminoacyl moiety and tRNA acceptor stem by human (Homo sapiens, or Hs) ProXp-ala was examined. Enzymatic assays revealed that Hs ProXp-ala requires C72 and C73 in the context of Hs cytosolic tRNAPro for efficient deacylation of mischarged Ala-tRNAPro. The strong dependence on these bases prevents cross-species deacylation of bacterial Ala-tRNAPro or of Hs mitochondrial Ala-tRNAPro by the human enzyme. Similar to the bacterial enzyme, Hs ProXp-ala showed strong tRNA acceptor-stem recognition but differed in its amino acid specificity profile relative to bacterial ProXp-ala. Changes at conserved residues in both the Hs and bacterial ProXp-ala substrate-binding pockets modulated this specificity. These results illustrate how the mechanism of substrate selection diverged during the evolution of the ProXp-ala family, providing the first example of a trans-editing domain whose specificity evolved to adapt to changes in its tRNA substrate.

Sign in / Sign up

Export Citation Format

Share Document