The aminoacyl-tRNA synthetases are prominently known for their classic function in the first step of protein synthesis, where they bear the responsibility of setting the genetic code. Each enzyme is exquisitely adapted to covalently link a single standard amino acid to its cognate set of tRNA isoacceptors. These ancient enzymes have evolved idiosyncratically to host alternate activities that go far beyond their aminoacylation role and impact a wide range of other metabolic pathways and cell signaling processes. The family of aminoacyl-tRNA synthetases has also been suggested as a remarkable scaffold to incorporate new domains that would drive evolution and the emergence of new organisms with more complex function. Because they are essential, the tRNA synthetases have served as pharmaceutical targets for drug and antibiotic development. The recent unfolding of novel important functions for this family of proteins offers new and promising pathways for therapeutic development to treat diverse human diseases.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4062602 | PMC |
| http://dx.doi.org/10.1002/wrna.1224 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Human disease-causing missense genetic variants are enriched in the evolutionarily ancient domains of the cytosolic aminoacyl-tRNA synthetase proteins.
IUBMB Life
January 2025
Department of Biology, Pomona College, Claremont, California, USA.
All life depends on accurate and efficient protein synthesis. The aminoacyl-tRNA synthetases (aaRSs) are a family of proteins that play an essential role in protein translation, as they catalyze the esterification reaction that charges a transfer RNA (tRNA) with its cognate amino acid. However, new domains added to the aaRSs over the course of evolution in eukaryotes confer novel functions unrelated to protein translation.
View Article and Find Full Text PDFTransfer RNA and small molecule therapeutics for aminoacyl-tRNA synthetase diseases.
FEBS J
December 2024
Department of Biochemistry, Schulich School of Medicine and Dentistry, Western University, London, Canada.
Aminoacyl-tRNA synthetases catalyze the ligation of a specific amino acid to its cognate tRNA. The resulting aminoacyl-tRNAs are indispensable intermediates in protein biosynthesis, facilitating the precise decoding of the genetic code. Pathogenic alleles in the aminoacyl-tRNA synthetases can lead to several dominant and recessive disorders.
View Article and Find Full Text PDFPhotosynthetic demands on translational machinery drive retention of redundant tRNA metabolism in plant organelles.
Proc Natl Acad Sci U S A
December 2024
Department of Biology, Colorado State University, Fort Collins, CO 80523.
Eukaryotic nuclear genomes often encode distinct sets of translation machinery for function in the cytosol vs. organelles (mitochondria and plastids). This raises questions about why multiple translation systems are maintained even though they are capable of comparable functions and whether they evolve differently depending on the compartment where they operate.
View Article and Find Full Text PDF[Analysis of clinical features of ruccrent interstitial lung disease in patients with anti-EJ positive antisynthetase syndrome].
Beijing Da Xue Xue Bao Yi Xue Ban
December 2024
Department of Rheumatology and Immunology, the First Affiliated Hospital of Nanjing Medical University, Nanjing 210029, China.
Objective: To summarize the clinical characteristics of 57 patients diagnosed with anti-glycyl tRNA synthetase (anti-EJ) positive antisynthetase syndrome (ASS), a subtype of anti-glycyl tRNA positive ASS, complicated by interstitial lung disease (ILD), and to investigate the factors asso-ciated with ILD recurrence.
Methods: A retrospective analysis was conducted on the clinical data of 57 anti-EJ positive ASS patientswho were treated at the First Affiliated Hospital of Nanjing Medical University from January 1, 2020 to June 30, 2024. The data collected included demographic information, clinical characteristics, laboratory test results, chest CT findings, and pulmonary function tests.
Mechanistic insights into the viral microorganism inactivation during lime stabilization for wastewater sludges.
J Hazard Mater
December 2024
Centre for Technology in Water and Wastewater, School of Civil and Environmental Engineering, University of Technology Sydney, Sydney, NSW 2007, Australia.
The pathogens inactivation in wastewater sludges is vitally important for safely managing solid wastes and protecting public and environmental health especially in the emergency. Reports have shown the effectiveness of lime to kill virus pathogens in sludges, but mechanism of virus inactivation and related human diseases is unclear. This study evaluated representative limes of CaO/CaO on actual viral microorganism inactivation by viral metagenomic sequencing technology.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!