Coupled amino acid vestiges of the primordial genetic code

1984 ◽  
Vol 14 (1-4) ◽  
pp. 589-596 ◽  
Author(s):  
Daniel Grafstein
Keyword(s):  
Amino Acid ◽  
Genetic Code ◽  
Primordial Genetic Code

scholarly journals Transferability of N-terminal mutations of pyrrolysyl-tRNA synthetase in one species to that in another species on unnatural amino acid incorporation efficiency

Amino Acids ◽  
2020 ◽  
Author(s):  
Thomas L. Williams ◽  
Debra J. Iskandar ◽  
Alexander R. Nödling ◽  
Yurong Tan ◽  
Louis Y. P. Luk ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Genetic Code ◽  
Unnatural Amino Acids ◽  
Trna Synthetase ◽  
Unnatural Amino Acid ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Genetic Code Expansion ◽  
Incorporation Efficiency

AbstractGenetic code expansion is a powerful technique for site-specific incorporation of an unnatural amino acid into a protein of interest. This technique relies on an orthogonal aminoacyl-tRNA synthetase/tRNA pair and has enabled incorporation of over 100 different unnatural amino acids into ribosomally synthesized proteins in cells. Pyrrolysyl-tRNA synthetase (PylRS) and its cognate tRNA from Methanosarcina species are arguably the most widely used orthogonal pair. Here, we investigated whether beneficial effect in unnatural amino acid incorporation caused by N-terminal mutations in PylRS of one species is transferable to PylRS of another species. It was shown that conserved mutations on the N-terminal domain of MmPylRS improved the unnatural amino acid incorporation efficiency up to five folds. As MbPylRS shares high sequence identity to MmPylRS, and the two homologs are often used interchangeably, we examined incorporation of five unnatural amino acids by four MbPylRS variants at two temperatures. Our results indicate that the beneficial N-terminal mutations in MmPylRS did not improve unnatural amino acid incorporation efficiency by MbPylRS. Knowledge from this work contributes to our understanding of PylRS homologs which are needed to improve the technique of genetic code expansion in the future.

scholarly journals Ribosome Evolution and Structural Capacitance

2019 ◽  
Author(s):  
Ashley M Buckle ◽  
Malcolm Buckle
Keyword(s):  
Amino Acid ◽  
Genetic Code ◽  
Protein Evolution ◽  
Bioinformatic Analysis ◽  
Amino Acid Usage ◽  
Loss Of Function ◽  
Gain Of Function ◽  
Acceptor Stem ◽  
Ribosome Evolution ◽  
Disordered Regions

In addition to the canonical loss-of-function mutations, mutations in proteins may additionally result in gain-of-function through the binary activation of cryptic ‘structural capacitance elements’. Our previous bioinformatic analysis allowed us to propose a new mechanism of protein evolution - structural capacitance – that arises via the generation of new elements of microstructure upon mutations that cause a disorder-to-order (DO) transition in previously disordered regions of proteins. Here we propose that the DO transition is a necessary follow-on from expected early codon-anticodon and tRNA acceptor stem-amino acid usage, via the accumulation of structural capacitance elements - reservoirs of disorder in proteins. We develop this argument further to posit that structural capacitance is an inherent consequence of the evolution of the genetic code.

Structure of the genetic code suggested by the hydropathy correlation between anticodons and amino acid residues

2006 ◽  
Vol 37 (1) ◽  
pp. 83-103 ◽  
Author(s):  
Sávio Torres de Farias ◽  
Carlos Henrique Costa Moreira ◽  
Romeu Cardoso Guimarães
Keyword(s):  
Amino Acid ◽  
Genetic Code ◽  
Amino Acid Residues

A plausible model correlates prebiotic peptide synthesis with the primordial genetic code

2018 ◽  
Vol 54 (62) ◽  
pp. 8598-8601 ◽  
Author(s):  
Jianxi Ying ◽  
Songsen Fu ◽  
Xin Li ◽  
Liubin Feng ◽  
Pengxiang Xu ◽  
...  
Keyword(s):  
Genetic Code ◽  
Peptide Synthesis ◽  
Plausible Model ◽  
Primordial Genetic Code ◽  
Prebiotic Peptide Synthesis

The analogs of 5′-aa-AMPs, namely nucleotide amidates (aa-N-NMPs), obtained under Hadean conditions. B = base.

scholarly journals The structural basis of the genetic code: amino acid recognition by aminoacyl-tRNA synthetases

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Florian Kaiser ◽  
Sarah Krautwurst ◽  
Sebastian Salentin ◽  
V. Joachim Haupt ◽  
Christoph Leberecht ◽  
...  
Keyword(s):  
Amino Acid ◽  
Genetic Code ◽  
Structural Basis ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Amino Acid Recognition
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