Aminoacyl-tRNA synthetases
MAR Gomez, M Ibba - Rna, 2020 - rnajournal.cshlp.org
The aminoacyl-tRNA synthetases are an essential and universally distributed family of
enzymes that plays a critical role in protein synthesis, pairing tRNAs with their cognate …
enzymes that plays a critical role in protein synthesis, pairing tRNAs with their cognate …
Biochemistry of aminoacyl tRNA Synthetase and tRNAs and their engineering for cell-free and synthetic cell applications
RB Ganesh, SJ Maerkl - Frontiers in bioengineering and …, 2022 - frontiersin.org
Cell-free biology is increasingly utilized for engineering biological systems, incorporating
novel functionality, and circumventing many of the complications associated with cells. The …
novel functionality, and circumventing many of the complications associated with cells. The …
A genomic database furnishes minimal functional glycyl-tRNA synthetases homologous to other, designed class II urzymes
The hypothesis that conserved core catalytic sites could represent ancestral aminoacyl-
tRNA synthetases (AARS) drove the design of functional TrpRS, LeuRS, and HisRS …
tRNA synthetases (AARS) drove the design of functional TrpRS, LeuRS, and HisRS …
The complex evolutionary history of aminoacyl-tRNA synthetases
Aminoacyl-tRNA synthetases (AARSs) are a superfamily of enzymes responsible for the
faithful translation of the genetic code and have lately become a prominent target for …
faithful translation of the genetic code and have lately become a prominent target for …
AARS Online: A collaborative database on the structure, function, and evolution of the aminoacyl‐tRNA synthetases
The aminoacyl‐tRNA synthetases (aaRS) are a large group of enzymes that implement the
genetic code in all known biological systems. They attach amino acids to their cognate …
genetic code in all known biological systems. They attach amino acids to their cognate …
The enigmatic genome of an obligate ancient Spiroplasma symbiont in a hadal holothurian
LS He, PW Zhang, JM Huang, FC Zhu… - Applied and …, 2018 - Am Soc Microbiol
Protective symbiosis has been reported in many organisms, but the molecular mechanisms
of the mutualistic interactions between the symbionts and their hosts are unclear. Here, we …
of the mutualistic interactions between the symbionts and their hosts are unclear. Here, we …
The binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements
L Han, Z Luo, Y Ju, B Chen, T Zou, J Wang, J Xu… - Science …, 2023 - science.org
As a class of essential enzymes in protein translation, aminoacyl–transfer RNA (tRNA)
synthetases (aaRSs) are organized into two classes of 10 enzymes each, based on two …
synthetases (aaRSs) are organized into two classes of 10 enzymes each, based on two …
[HTML][HTML] Genomic database furnishes a spontaneous example of a functional Class II glycyl-tRNA synthetase urzyme
The chief barrier to studies of how genetic coding emerged is the lack of experimental
models for ancestral aminoacyl-tRNA synthetases (AARS). We hypothesized that conserved …
models for ancestral aminoacyl-tRNA synthetases (AARS). We hypothesized that conserved …
X-shaped structure of bacterial heterotetrameric tRNA synthetase suggests cryptic prokaryote functions and a rationale for synthetase classifications
Y Ju, L Han, B Chen, Z Luo, Q Gu, J Xu… - Nucleic Acids …, 2021 - academic.oup.com
AaRSs (aminoacyl-tRNA synthetases) group into two ten-member classes throughout
evolution, with unique active site architectures defining each class. Most are monomers or …
evolution, with unique active site architectures defining each class. Most are monomers or …
Aminoacyl-tRNA synthetase evolution and sectoring of the genetic code
D Pak, Y Kim, ZF Burton - Transcription, 2018 - Taylor & Francis
The genetic code sectored via tRNA charging errors, and the code progressed toward
closure and universality because of evolution of aminoacyl-tRNA synthetase (aaRS) fidelity …
closure and universality because of evolution of aminoacyl-tRNA synthetase (aaRS) fidelity …