Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases

Biochemistry ◽  
1975 ◽  
Vol 14 (1) ◽  
pp. 1-4 ◽  
Author(s):  
Alan R. Fersht ◽  
Jeremy S. Ashford ◽  
Christopher J. Bruton ◽  
Ross Jakes ◽  
Gordon L. E. Koch ◽  
...  
Keyword(s):  
Active Site ◽  
Trna Synthetases ◽  
Binding Stoichiometry ◽  
Aminoacyl Trna Synthetases

The class II aminoacyl-tRNA synthetases and their active site: Evolutionary conservation of an ATP binding site

1995 ◽  
Vol 40 (5) ◽  
Author(s):  
Gilbert Eriani ◽  
Jean Cavarelli ◽  
Franck Martin ◽  
Laurent Ador ◽  
Bernard Rees ◽  
...  
Keyword(s):  
Binding Site ◽  
Active Site ◽  
Evolutionary Conservation ◽  
Class Ii ◽  
Atp Binding ◽  
Atp Binding Site ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases

scholarly journals Plasticity and Constraints of tRNA Aminoacylation Define Directed Evolution of Aminoacyl-tRNA Synthetases

2019 ◽  
Vol 20 (9) ◽  
pp. 2294 ◽  
Author(s):  
Ana Crnković ◽  
Oscar Vargas-Rodriguez ◽  
Dieter Söll
Keyword(s):  
Amino Acids ◽  
Directed Evolution ◽  
Active Site ◽  
Nonsense Suppression ◽  
Natural Amino Acid ◽  
Noncanonical Amino Acids ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Genetic Incorporation

Genetic incorporation of noncanonical amino acids (ncAAs) has become a powerful tool to enhance existing functions or introduce new ones into proteins through expanded chemistry. This technology relies on the process of nonsense suppression, which is made possible by directing aminoacyl-tRNA synthetases (aaRSs) to attach an ncAA onto a cognate suppressor tRNA. However, different mechanisms govern aaRS specificity toward its natural amino acid (AA) substrate and hinder the engineering of aaRSs for applications beyond the incorporation of a single l-α-AA. Directed evolution of aaRSs therefore faces two interlinked challenges: the removal of the affinity for cognate AA and improvement of ncAA acylation. Here we review aspects of AA recognition that directly influence the feasibility and success of aaRS engineering toward d- and β-AAs incorporation into proteins in vivo. Emerging directed evolution methods are described and evaluated on the basis of aaRS active site plasticity and its inherent constraints.

scholarly journals Virus-Encoded Aminoacyl-tRNA Synthetases: Structural and Functional Characterization of Mimivirus TyrRS and MetRS

2007 ◽  
Vol 81 (22) ◽  
pp. 12406-12417 ◽  
Author(s):  
Chantal Abergel ◽  
Joëlle Rudinger-Thirion ◽  
Richard Giegé ◽  
Jean-Michel Claverie
Keyword(s):  
Active Site ◽  
Functional Characterization ◽  
Evolutionary Relationship ◽  
Trna Synthetase ◽  
Dna Viruses ◽  
Trna Synthetases ◽  
Functional Studies ◽  
Aminoacyl Trna Synthetases ◽  
Viral Enzyme

ABSTRACT Aminoacyl-tRNA synthetases are pivotal in determining how the genetic code is translated in amino acids and in providing the substrate for protein synthesis. As such, they fulfill a key role in a process universally conserved in all cellular organisms from their most complex to their most reduced parasitic forms. In contrast, even complex viruses were not found to encode much translation machinery, with the exception of isolated components such as tRNAs. In this context, the discovery of four aminoacyl-tRNA synthetases encoded in the genome of mimivirus together with a full set of translation initiation, elongation, and termination factors appeared to blur what was once a clear frontier between the cellular and viral world. Functional studies of two mimivirus tRNA synthetases confirmed the MetRS specificity for methionine and the TyrRS specificity for tyrosine and conformity with the identity rules for tRNATyr for archea/eukarya. The atomic structure of the mimivirus tyrosyl-tRNA synthetase in complex with tyrosinol exhibits the typical fold and active-site organization of archaeal-type TyrRS. However, the viral enzyme presents a unique dimeric conformation and significant differences in its anticodon binding site. The present work suggests that mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas. Their phylogenetic classification does not suggest that they have been acquired recently by horizontal gene transfer from a cellular host but rather militates in favor of an intricate evolutionary relationship between large DNA viruses and ancestral eukaryotes.

Analytical strategy for determination of active site sequences in aminoacyl-tRNA synthetases

1988 ◽  
Vol 438 ◽  
pp. 347-357 ◽  
Author(s):  
Christian Beauvallet ◽  
Codjo Hountondji ◽  
Jean-Marie Schmitter
Keyword(s):  
Active Site ◽  
Analytical Strategy ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases
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