Evolution of function of a fused metazoan tRNA synthetase.
@article{Ray2011EvolutionOF, title={Evolution of function of a fused metazoan tRNA synthetase.}, author={Partho Sarothi Ray and James C. Sullivan and Jie Jia and John Francis and John R. Finnerty and Paul L. Fox}, journal={Molecular biology and evolution}, year={2011}, volume={28 1}, pages={ 437-47 } }
The origin and evolution of multidomain proteins are driven by diverse processes including fusion/fission, domain shuffling, and alternative splicing. The 20 aminoacyl-tRNA synthetases (AARS) constitute an ancient conserved family of multidomain proteins. The glutamyl-prolyl tRNA synthetase (EPRS) of bilaterian animals is unique among AARSs, containing two functional enzymes catalyzing ligation of glutamate and proline to their cognate transfer RNAs (tRNAs). The ERS and PRS catalytic domains in…
23 Citations
Origin and Evolution of Glutamyl-prolyl tRNA Synthetase WHEP Domains Reveal Evolutionary Relationships within Holozoa
- BiologyPloS one
- 2014
Investigating the duplications, deletions and divergence of WHEP domains, the bifunctional EPRS is traced to choanozoans and the fusion event leading to its origin at the divergence of ichthyosporea and emergence of filozoa nearly a billion years ago is identified.
Aminoacyl-tRNA Synthetases in the Bacterial World.
- BiologyEcoSal Plus
- 2016
Comparisons and differences in the properties of aaRSs from the three kingdoms of life are pinpointed throughout the review and distinctive characteristics of bacterium-like synthetases from organelles are outlined.
Evolution of the multi-tRNA synthetase complex and its role in cancer
- BiologyThe Journal of Biological Chemistry
- 2019
It is proposed that the regulatory activities of the MSC-associated ARSs mainly converge on five biological processes, including mammalian target of rapamycin (mTOR) and DNA repair pathways, and how aberrant or disrupted interactions in the M SC can cause disease.
The zinc-binding domain of mammalian prolyl-tRNA synthetase is indispensable for catalytic activity and organism viability
- Biology, ChemistryiScience
- 2021
Non-catalytic regulation of gene expression by aminoacyl-tRNA synthetases.
- BiologyTopics in current chemistry
- 2014
This chapter considers the non-canonical functions of AARSs in regulating gene expression by mechanisms not directly related to their enzymatic activities, namely, at the levels of mRNA production, processing, and translation.
Metabolic origin of the fused aminoacyl-tRNA synthetase, glutamyl-prolyl-tRNA synthetase
- BiologyThe Journal of Biological Chemistry
- 2018
It is proposed here that a confluence of metabolic, biochemical, and environmental factors contributed to the specific fusion of glutamyl- (ERS) and prolyl- (PRS) tRNA synthetases, resulting in marked cellular depletion of glutamic acid and its products.
Evolutionary gain of highly divergent tRNA specificities by two isoforms of human histidyl-tRNA synthetase
- BiologyCellular and Molecular Life Sciences
- 2017
This study suggests that the human HisRS genes, while descending from a common ancestor with dual function for both types of tRNAHis, have acquired highly specialized tRNA recognition properties through evolution.
Architecture and metamorphosis.
- BiologyTopics in current chemistry
- 2014
The MSC has been proposed to have a functional dualism: facilitating protein synthesis and serving as a reservoir of non-canonical functions associated with its synthetase and non-synthetase components and domain additions and functional expansions are found in almost all aaRS proteins.
Essential nontranslational functions of tRNA synthetases.
- Biology, ChemistryNature chemical biology
- 2013
The expropriation of aaRSs for essential nontranslational functions may have been initiated by co-opting the amino acid-binding site for another purpose.
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