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Engineered initiator tRNAs can effectively start translation at non-AUG start codons and diversify N-terminal amino acids for mRNA Display.
Nucleic Acids Res
January 2025
Department of Peptide Therapeutics, Genentech, South San Francisco, CA 94080, USA.
mRNA display is an effective tool to identify high-affinity macrocyclic binders for challenging protein targets. The success of an mRNA display selection is dependent on generating highly diverse libraries with trillions of peptides. While translation elongation can canonically accommodate the 61 proteinogenic triplet codons, translation initiation is restricted to the native start codon AUG.
View Article and Find Full Text PDFStructural basis for aminoacylation of cellular modified tRNA by human lysyl-tRNA synthetase.
bioRxiv
December 2024
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven CT, 06511, USA.
The average eukaryotic tRNA contains 13 posttranscriptional modifications; however, their functional impact is largely unknown. Our understanding of the complex tRNA aminoacylation machinery in metazoans also remains limited. Herein, using a series of high-resolution cryo-electron microscopy (cryo-EM) structures, we provide the mechanistic basis for recognition and aminoacylation of fully-modified cellular tRNA by human lysyl-tRNA synthetase (h-LysRS).
View Article and Find Full Text PDFMechanism of Catalysis and Substrate Binding of Epoxyqueuosine Reductase in the Biosynthetic Pathway to Queuosine-Modified tRNA.
Biochemistry
January 2025
Department of Chemistry, University of Florida, Gainesville, Florida 32611, United States.
Post-transcriptional modifications at the anticodon stem-loop of tRNAs are key to the translation function. Metabolic pathways to these modifications often incorporate complex enzymology. A notable example is the hypermodified nucleoside, queuosine, found at the wobble position of Asn, Asp, His, and Tyr encoding tRNAs.
View Article and Find Full Text PDFStructure-function analysis of tRNA tA-catalysis, assembly, and thermostability of Aquifex aeolicus TsaDB tetramer in complex with TsaE.
J Biol Chem
December 2024
School of Life Sciences, Key Laboratory of Cell Activities and Stress Adaptation of the Ministry of Education, Lanzhou University, Lanzhou, China. Electronic address:
Article Synopsis
- The modification of tRNA at position 37 (tA) is crucial for ensuring accurate protein synthesis and is produced through the actions of specific enzymes (TsaC, TsaD, TsaB, and TsaE) using L-threonine and ATP in bacteria.
- This study reconstituted the biosynthesis of tA from the bacterium Aquifex aeolicus and examined the structural characteristics of the TsaDB enzyme complex, finding that it can bind both TsaE and tRNA, with the binding being influenced by specific protein sequences.
- The research showed that TsaE enhances the catalytic action of TsaDB, leading to the release of tRNA
Biochemical and structural insights into a 5' to 3' RNA ligase reveal a potential role in tRNA ligation.
Proc Natl Acad Sci U S A
October 2024
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Article Synopsis
- ATP-grasp superfamily enzymes have a hand-like structure and perform various reactions using a similar catalytic mechanism, with over 30 families linked to cellular functions and diseases.
- The study identifies C12orf29 (RLIG1) as a unique ATP-grasp enzyme that ligates RNA, specifically targeting RNA halves with certain chemical groups.
- Research indicates that RLIG1 impacts tRNA levels in knockout mice, especially in females, and possesses a distinct RNA ligase structure that plays a crucial role in tRNA biology.
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