Works (5)

Updated: July 5th, 2023 15:54

2012 journal article

Human tRNA(UUU)(LYs3) Is Pre-Structured by Natural Modifications for Cognate and Wobble Codon Binding through Keto-Enol Tautomerism


By: F. Vendeix n, F. Murphy*, W. Cantara n, G. Leszczynska*, E. Gustilo n, B. Sproat, A. Malkiewicz*, P. Agris n

author keywords: modifications; wobble decoding; anticodon structure; tRNA(LYs3)
MeSH headings : Anticodon / chemistry; Base Pairing; Circular Dichroism; Codon / chemistry; Crystallography, X-Ray; Humans; Hydrogen Bonding; Models, Molecular; Nucleic Acid Conformation; Pseudouridine / chemistry; RNA, Transfer, Lys / chemistry; Thermodynamics; Thiouridine / analogs & derivatives; Thiouridine / chemistry
TL;DR: The results unambiguously demonstrate that modifications pre-structure the anticodon as a key prerequisite for efficient and accurate recognition of cognate and wobble codons. (via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being (Web of Science; OpenAlex)
Source: Web Of Science
Added: August 6, 2018

2008 journal article

Anticodon domain modifications contribute order to tRNA for ribosome-mediated codon binding

BIOCHEMISTRY, 47(23), 6117–6129.

By: F. Vendeix n, A. Dziergowska n, E. Gustilo n, W. Graham n, B. Sproat n, A. Malkiewicz n, P. Agris n

MeSH headings : Anticodon / chemistry; Base Sequence; Binding Sites; Codon / chemistry; Codon / metabolism; Dinucleoside Phosphates / chemistry; Escherichia coli / genetics; Magnetic Resonance Spectroscopy; Nucleic Acid Conformation; Oligoribonucleotides / chemistry; RNA, Bacterial / chemistry; RNA, Bacterial / genetics; RNA, Transfer / genetics; Ribosomes / metabolism
TL;DR: Results clearly demonstrate that the xo (5)U 34-type modifications order the anticodon loop prior to A-site codon binding for an expanded codon reading, possibly reducing an entropic energy barrier to codonbinding. (via Semantic Scholar)
UN Sustainable Development Goal Categories
7. Affordable and Clean Energy (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

2008 journal article

Synthesis and investigation of the 5-formylcytidine modified, anticodon stem and loop of the human mitochondrial tRNA(Met)

NUCLEIC ACIDS RESEARCH, 36(20), 6548–6557.

By: H. Lusic n, E. Gustilo n, F. Vendeix n, R. Kaiser n, M. Delaney n, W. Graham n, V. Moye n, W. Cantara n, P. Agris n, A. Deiters n

MeSH headings : Anticodon / chemistry; Base Sequence; Codon / metabolism; Cytidine / analogs & derivatives; Cytidine / chemistry; Humans; Molecular Sequence Data; Nucleic Acid Conformation; Protein Biosynthesis; RNA / chemistry; RNA, Mitochondrial; RNA, Transfer, Met / chemical synthesis; RNA, Transfer, Met / chemistry; RNA, Transfer, Met / metabolism; Thermodynamics
TL;DR: The first synthesis and analyses of the tRNA's anticodon stem and loop domain containing the 5-formylcytidine modification are reported, contributing to the tRNAs anticodon domain structure, thermodynamic properties and its ability to bind codons AUA and AUG in translational initiation and elongation. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2008 review

tRNA's modifications bring order to gene expression

[Review of ]. Current Opinion in Microbiology, 11(2), 134–140.

By: E. Gustilo, A. Franck & P. Agris

Source: NC State University Libraries
Added: August 6, 2018

2007 journal article

E-coli glutamyl-tRNA synthetase is inhibited by anticodon stem-loop domains and a minihelix

RNA BIOLOGY, 4(2), 85–92.

By: E. Gustilo n, D. Dubois, J. Lapointe & P. Agris*

author keywords: designed inhibitors; RNA fragments; competitive inhibitors; identity elements; modified RNA; translation
MeSH headings : Anticodon / chemistry; Base Sequence; Binding Sites; Enzyme Inhibitors / chemistry; Escherichia coli / enzymology; Escherichia coli Proteins / antagonists & inhibitors; Escherichia coli Proteins / metabolism; Glutamate-tRNA Ligase / antagonists & inhibitors; Glutamate-tRNA Ligase / metabolism; Molecular Sequence Data; Nucleic Acid Conformation; RNA, Transfer / chemistry; Thermodynamics; Transfer RNA Aminoacylation; Uridine / analogs & derivatives; Uridine / chemistry
TL;DR: The modified ASLGlu-s2U34, though having a higher affinity for ERS, may be released more readily and thus, not be as good an inhibitor as the unmodified ASL, but the RNA constructs are effective tools to study RNA-protein interaction. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

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