scholarly journals Interstrand Aminoacyl Transfer in a tRNA Acceptor Stem-Overhang Mimic

2021 ◽  
Author(s):  
Long-Fei Wu ◽  
Meng Su ◽  
Ziwei Liu ◽  
Samuel J. Bjork ◽  
John D. Sutherland
Keyword(s):  
Acceptor Stem ◽  
Aminoacyl Transfer ◽  
Trna Acceptor

scholarly journals Adaptation to tRNA acceptor stem structure by flexible adjustment in the catalytic domain of class I tRNA synthetases

RNA ◽  
2011 ◽  
Vol 18 (2) ◽  
pp. 213-221 ◽  
Author(s):  
C. Liu ◽  
J. M. Sanders ◽  
J. M. Pascal ◽  
Y.-M. Hou
Keyword(s):  
Catalytic Domain ◽  
Class I ◽  
Trna Synthetases ◽  
Acceptor Stem ◽  
Stem Structure ◽  
Trna Acceptor

scholarly journals NMR analysis of tRNA acceptor stem microhelices: discriminator base change affects tRNA conformation at the 3' end.

1994 ◽  
Vol 91 (24) ◽  
pp. 11467-11471 ◽  
Author(s):  
E. V. Puglisi ◽  
J. D. Puglisi ◽  
J. R. Williamson ◽  
U. L. RajBhandary
Keyword(s):  
Base Change ◽  
Nmr Analysis ◽  
Acceptor Stem ◽  
Discriminator Base ◽  
Trna Acceptor

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.

scholarly journals tRNA acceptor-stem and anticodon bases embed separate features of amino acid chemistry

RNA Biology ◽  
2015 ◽  
Vol 13 (2) ◽  
pp. 145-151 ◽  
Author(s):  
Charles W. Carter ◽  
Richard Wolfenden
Keyword(s):  
Amino Acid ◽  
Acceptor Stem ◽  
Trna Acceptor

scholarly journals Two Classes of tRNA Synthetases Suggested by Sterically Compatible Dockings on tRNA Acceptor Stem

Cell ◽  
2001 ◽  
Vol 104 (2) ◽  
pp. 191-193 ◽  
Author(s):  
Lluís Ribas de Pouplana ◽  
Paul Schimmel
Keyword(s):  
Trna Synthetases ◽  
Acceptor Stem ◽  
Trna Acceptor
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