Role of aminoacyl-tRNA-synthetases in changes in rate of protein biosynthesis in rabbit liver during myocardial ischemia

The genetic code defines how information in the genome is translated into protein. Aside from a handful of isolated exceptions, this code is universal. Researchers have developed techniques to artificially expand the genetic code, repurposing codons and translational machinery to incorporate nonstandard amino acids (nsAAs) into proteins. A key challenge for robust genetic code expansion is orthogonality; the engineered machinery used to introduce nsAAs into proteins must co-exist with native translation and gene expression without cross-reactivity or pleiotropy. The issue of orthogonality manifests at several levels, including those of codons, ribosomes, aminoacyl-tRNA synthetases, tRNAs, and elongation factors. In this concept paper, we describe advances in genome recoding, translational engineering and associated challenges rooted in establishing orthogonality needed to expand the genetic code.

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The Role of Aminoacyl-tRNA Synthetases in Genetic Diseases

Annual Review of Genomics and Human Genetics ◽

10.1146/annurev.genom.9.081307.164204 ◽

2008 ◽

Vol 9 (1) ◽

pp. 87-107 ◽

Cited By ~ 165

Author(s):

Anthony Antonellis ◽

Eric D. Green

Keyword(s):

Genetic Diseases ◽

Trna Synthetases ◽

Aminoacyl Trna Synthetases

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tRNA Synthetases Are Recruited to Yeast Ribosomes by rRNA Expansion Segment 7L but Do Not Require Association for Functionality

Non-Coding RNA ◽

10.3390/ncrna7040073 ◽

2021 ◽

Vol 7 (4) ◽

pp. 73

Author(s):

Nina Krauer ◽

Robert Rauscher ◽

Norbert Polacek

Keyword(s):

Ribosome Biogenesis ◽

Protein Biosynthesis ◽

Ribosomal Subunit ◽

Trna Synthetase ◽

Translation Efficiency ◽

Functional Roles ◽

Trna Synthetases ◽

Yeast Ribosomes ◽

Ribosome Association

Protein biosynthesis is essential for any organism, yet how this process is regulated is not fully understood at the molecular level. During evolution, ribosomal RNA expanded in specific regions, referred to as rRNA expansion segments (ES). First functional roles of these expansions have only recently been discovered. Here we address the role of ES7La located in the large ribosomal subunit for factor recruitment to the yeast ribosome and the potential consequences for translation. Truncation of ES7La has only minor effects on ribosome biogenesis, translation efficiency and cell doubling. Using yeast rRNA deletion strains coupled with ribosome-specific mass spectrometry we analyzed the interactome of ribosomes lacking ES7La. Three aminoacyl-tRNA synthetases showed reduced ribosome association. Synthetase activities however remained unaltered suggesting that the pool of aminoacylated tRNAs is unaffected by the ES deletion. These results demonstrated that aminoacylation activities of tRNA synthetases per se do not rely on ribosome association. These findings suggest a role of ribosome-associated aminoacyl-tRNA synthetase beyond their core enzymatic functions.

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