Relevant bibliographies by topics / TRNA Structure

Academic literature on the topic 'TRNA Structure'

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Published: 6 September 2023
Last updated: 7 September 2023

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Journal articles on the topic "TRNA Structure"

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Fiteha, Yosur G., and Mahmoud Magdy. "The Evolutionary Dynamics of the Mitochondrial tRNA in the Cichlid Fish Family." Biology 11, no. 10 (October 18, 2022): 1522. http://dx.doi.org/10.3390/biology11101522.

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The mitochondrial transfer RNA genes (tRNAs) attract more attention due to their highly dynamic and rapidly evolving nature. The current study aimed to detect and evaluate the dynamics, characteristic patterns, and variations of mitochondrial tRNAs. The study was conducted in two main parts: first, the published mitogenomic sequences of cichlids mt tRNAs have been filtered. Second, the filtered mitochondrial tRNA and additional new mitogenomes representing the most prevalent Egyptian tilapiine were compared and analyzed. Our results revealed that all 22 tRNAs of cichlids folded into a classical cloverleaf secondary structure with four domains, except for trnSGCU, missing the D domain in all cichlids. When consensus tRNAs were compared, most of the mutations were observed in the trnP at nucleotide levels (substitutions and indels), in contrast to trnLUAA. From a structural perspective, the anticodon loop and T-loop formations were the most conserved structures among all parts of the tRNA in contrast to the A-stem and D-loop formations. The trnW was the lowest polymorphic unneutral tRNA among all cichlids (both the family and the haplotilapiine lineage), in contrast with the neutral trnD that was extremely polymorphic among and within the haplotilapiine lineage species compared to other cichlids species. From a phylogenetic perspective, the trnC was extremely hypervariable and neutral tRNA in both haplotilapiine lineage and cichlids but was unable to report correct phylogenetic signal for the cichlids. In contrast to trnI and trnY, less variable neutral tRNAs that were able to cluster the haplotilapiine lineage and cichlids species as previously reported. By observing the DNA polymorphism in the coding DNA sequences (CDS), the highest affected amino acid by non-synonymous mutations was isoleucine and was equally mutated to valine and vice versa; no correlation between mutations in CDS and tRNAs was statistically found. The current study provides an insight into the mitochondrial tRNA evolution and its effect on the cichlid diversity and speciation model at the maternal level.
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Urbonavičius, Jaunius, Jérôme M. B. Durand, and Glenn R. Björk. "Three Modifications in the D and T Arms of tRNA Influence Translation in Escherichia coli and Expression of Virulence Genes in Shigella flexneri." Journal of Bacteriology 184, no. 19 (October 1, 2002): 5348–57. http://dx.doi.org/10.1128/jb.184.19.5348-5357.2002.

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ABSTRACT The modified nucleosides 2′-O-methylguanosine, present at position 18 (Gm18), 5-methyluridine, present at position 54 (m5U54), and pseudouridine, present at position 55 (Ψ55), are located in the D and T arms of tRNAs and are close in space in the three-dimensional (3D) structure of this molecule in the bacterium Escherichia coli. The formation of these modified nucleosides is catalyzed by the products of genes trmH (Gm18), trmA (m5U54), and truB (Ψ55). The combination of trmH, trmA, and truB mutations resulting in lack of these three modifications reduced the growth rate, especially at high temperature. Moreover, the lack of three modified nucleotides in tRNA induced defects in the translation of certain codons, sensitivity to amino acid analog 3,4-dehydro-dl-proline, and an altered oxidation of some carbon compounds. The results are consistent with the suggestion that these modified nucleosides, two of which directly interact in the 3D structure of tRNA by forming a hydrogen bond between Ψ55 and Gm18, stabilize the structure of the tRNA. Moreover, lack of Ψ55 in tRNA of human pathogen Shigella flexneri leads to a reduced expression of several virulence-associated genes.
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Mangroo, Dev, Xin-Qi Wu, and Uttam L. Rajbhandary. "Escherichia coliinitiator tRNA: structure–function relationships and interactions with the translational machinery." Biochemistry and Cell Biology 73, no. 11-12 (December 1, 1995): 1023–31. http://dx.doi.org/10.1139/o95-109.

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We showed previously that the sequence and (or) structural elements important for specifying the many distinctive properties of Escherichia coli initiator tRNA are clustered in the acceptor stem and in the anticodon stem and loop. This paper briefly describes this and reviews the results of some recently published studies on the mutant initiator tRNAs generated during this work. First, we have studied the effect of overproduction of methionyl-tRNA transformylase (MTF) and initiation factors IF2 and IF3 on activity of mutant initiator tRNAs mat are defective at specific steps in the initiation pathway. Overproduction of MTF rescued specifically the activity of mutant tRNAs defective in formylation but not mutants defective in binding to the P site. Overproduction of IF2 increased me activity of all mutant tRNAs having the CUA anticodon but not of mutant tRNA having me GAC anticodon. Overproduction of IF3 had no effect on the activity of any of me mutant tRNAs tested. Second, for functional studies of mutant initiator tRNA in vivo, we used a CAU→CUA anticodon sequence mutant mat can initiate protein synthesis from UAG instead of AUG. In contrast with me wild-type initiator tRNA, the mutant initiator tRNA has a 2-methylthio-N6-isopentenyl adenosine (ms2i6A) base modification next to the anticodon. Interestingly, this base modification is now important for activity of the mutant tRNA in initiation. In a miaA strain of E. coli deficient in biosynthesis of ms2i6A, the mutant initiator tRNA is much less active in initiation. The defect is specifically in binding to the ribosomal P site.Key words: initiator tRNA, initiation Factors, formylation, P site binding, base modification.
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Teramoto, Takamasa, Kipchumba J. Kaitany, Yoshimitsu Kakuta, Makoto Kimura, Carol A. Fierke, and Traci M. Tanaka Hall. "Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA." Nucleic Acids Research 48, no. 21 (July 28, 2020): 11815–26. http://dx.doi.org/10.1093/nar/gkaa627.

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Abstract Pentatricopeptide repeat (PPR) motifs are α-helical structures known for their modular recognition of single-stranded RNA sequences with each motif in a tandem array binding to a single nucleotide. Protein-only RNase P 1 (PRORP1) in Arabidopsis thaliana is an endoribonuclease that uses its PPR domain to recognize precursor tRNAs (pre-tRNAs) as it catalyzes removal of the 5′-leader sequence from pre-tRNAs with its NYN metallonuclease domain. To gain insight into the mechanism by which PRORP1 recognizes tRNA, we determined a crystal structure of the PPR domain in complex with yeast tRNAPhe at 2.85 Å resolution. The PPR domain of PRORP1 bound to the structurally conserved elbow of tRNA and recognized conserved structural features of tRNAs using mechanisms that are different from the established single-stranded RNA recognition mode of PPR motifs. The PRORP1 PPR domain-tRNAPhe structure revealed a conformational change of the PPR domain upon tRNA binding and moreover demonstrated the need for pronounced overall flexibility in the PRORP1 enzyme conformation for substrate recognition and catalysis. The PRORP1 PPR motifs have evolved strategies for protein-tRNA interaction analogous to tRNA recognition by the RNA component of ribonucleoprotein RNase P and other catalytic RNAs, indicating convergence on a common solution for tRNA substrate recognition.
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Chiang, C. C., and A. M. Lambowitz. "The Mauriceville retroplasmid reverse transcriptase initiates cDNA synthesis de novo at the 3' end of tRNAs." Molecular and Cellular Biology 17, no. 8 (August 1997): 4526–35. http://dx.doi.org/10.1128/mcb.17.8.4526.

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The Mauriceville retroplasmid of Neurospora mitochondria encodes a novel reverse transcriptase that initiates cDNA synthesis de novo (i.e., without a primer) at the 3' CCA of the plasmid transcript's 3' tRNA-like structure (H. Wang and A. M. Lambowitz, Cell 75:1071-1081, 1993). Here, we show that the plasmid reverse transcriptase also initiates cDNA synthesis de novo at the 3' end of tRNAs, leading to synthesis of a full-length cDNA copy of the tRNA. The use of tRNA templates in vivo was suggested previously by the structure of suppressive mutant plasmids that have incorporated mitochondrial tRNA sequences (R. A. Akins, R. L. Kelley, and A. M. Lambowitz, Cell 47:505-516, 1986). The in vitro experiments show that efficient de novo initiation on tRNA templates requires an unpaired 3' CCA and occurs predominantly opposite position C-2 of the 3' CCA sequence, the same position as in the plasmid transcript. In other reactions, the plasmid reverse transcriptase synthesizes cDNA dimers by template switching between two tRNA templates and initiates at an internal position in a tRNA by using the 3' end of the tRNA as a primer. Finally, we show that template switching between the tRNA and the plasmid transcript in vitro gives rise to hybrid cDNAs of the type predicted to be intermediates in the generation of the suppressive mutant plasmids. The ability of the plasmid reverse transcriptase to initiate at the 3' end of tRNAs presumably reflects the recognition of structural features similar to those of the 3' tRNA-like structure of the plasmid transcript. The recognition of tRNAs or tRNA-like structures as templates for cDNA synthesis may be characteristic of primitive reverse transcriptases that evolved from RNA-dependent RNA polymerases.
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Nakamura, Akiyoshi, Taiki Nemoto, Isao Tanaka, and Min Yao. "Structural analysis of tRNA(His) guanylyltransferase comlexed with tRNA." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1816. http://dx.doi.org/10.1107/s2053273314081844.

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tRNA(His) guanylyltransferase (Thg1) of eukaryote adds a guanylate to the 5' end of immature or incorrectly processed tRNAs (3'-5' polymerization) by three reaction steps: adenylylation; guanylylation and dephosphorylation. This additional guanylate provides the major identity element for histidyl-tRNA synthetase to recognize its cognate substrate tRNA(His) and differentiates tRNA(His) from the pool of tRNAs present in the cell (1). Previous studies indicate that Thg1 is a structural homolog of canonical 5'-3' polymerases in the catalytic core with no obvious conservation of the amino acid sequence(2). However, the substrate binding of Thg1 is unclear and requires information on the three-dimensional structure in complex with tRNA. In this study, we determined the crystal structures of Thg1 from Candida albicans (CaThg1) in tRNA-bound (CaThg1-tRNA), ATP-bound (CaThg1-ATP), and GTP-bound (CaThg1-GTP) form, and elucidated how Thg1 functions as a reverse polymerase to add nucleotide(3). The crystal structures of CaThg1-tRNA complex shows that two tRNAs are bound to tetrameric Thg1 in parallel orientation which is consistent with SAXS (Small angle X-ray scattering) and gel filtration analysis. One tRNA interacts with three monomers for its positioning, anticodon recognition, and catalytic activation. The end of the acceptor stem and the anticodon loop are both recognized by the same sub-domain belonging to the different monomers. Moreover, the structural comparison of Thg1-tRNA with canonical 5'-3' polymerase shows that the domain architecture of Thg1 is reversed to that of canonical 5'-3' polymerase.
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Hòa, Lê Thanh, Nguyễn Thị Khuê, Nguyễn Thị Bích Nga, Đỗ Thị Roan, Đỗ Trung Dũng, Lê Thị Kim Xuyến, and Đoàn Thị Thanh Hương. "Genetic characterization of mitochondrial genome of the small intestinal fluke, Haplorchis taichui (Trematoda: Heterophyidae), Vietnamese sample." Vietnam Journal of Biotechnology 14, no. 2 (June 30, 2016): 215–24. http://dx.doi.org/10.15625/1811-4989/14/2/9333.

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The small intestinal fluke, Haplorchis taichui Nishigori, 1924, belonging to genus Haplorchis (family Heterophyidae, class Trematoda, phylum Platyhelminthes), is a zoonotic pathogen causing disease in humans and animals. Complete mitochondrial genome (mtDNA) of H. taichui (strain HTAQT, collected from Quang Tri) was obtained and characterized for structural genomics providing valuable data for studies on epidemiology, species identification, diagnosis, classification, molecular phylogenetic relationships and prevention of the disease. The entire nucleotide mtDNA sequence of H. taichui (HTAQT) is 15.119 bp in length, containing 36 genes, including 12 protein-coding genes (cox1, cox2, cox3, nad1, nad2, nad3, nad4L, nad4, nad5, nad6, atp6 and cob); 2 ribosomal RNA genes, rrnL (16S) and rrnS (12S); 22 transfer RNA genes (tRNA or trn), and a non-coding region (NR), divided into two sub-regions of short non-coding (short, SNR) and long non-coding (long, LNR). LNR region, 1.692 bp in length, located between the position of trnG (transfer RNA-Glycine) and trnE (Glutamic acid), contains 6 tandem repeats (TR), arranged as TR1A, TR2A, TR1B, TR2B, TR3A, TR3B, respectively. Each protein coding gene (overall, 12 genes), ribosomal rRNA (2 genes) and tRNA (22 genes) were analyzed, in particular, protein-coding genes were defined in length, start and stop codons, and rRNA and tRNA genes for secondary structure.
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Ramos-Morales, Elizabeth, Efil Bayam, Jordi Del-Pozo-Rodríguez, Thalia Salinas-Giegé, Martin Marek, Peggy Tilly, Philippe Wolff, et al. "The structure of the mouse ADAT2/ADAT3 complex reveals the molecular basis for mammalian tRNA wobble adenosine-to-inosine deamination." Nucleic Acids Research 49, no. 11 (May 31, 2021): 6529–48. http://dx.doi.org/10.1093/nar/gkab436.

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Abstract Post-transcriptional modification of tRNA wobble adenosine into inosine is crucial for decoding multiple mRNA codons by a single tRNA. The eukaryotic wobble adenosine-to-inosine modification is catalysed by the ADAT (ADAT2/ADAT3) complex that modifies up to eight tRNAs, requiring a full tRNA for activity. Yet, ADAT catalytic mechanism and its implication in neurodevelopmental disorders remain poorly understood. Here, we have characterized mouse ADAT and provide the molecular basis for tRNAs deamination by ADAT2 as well as ADAT3 inactivation by loss of catalytic and tRNA-binding determinants. We show that tRNA binding and deamination can vary depending on the cognate tRNA but absolutely rely on the eukaryote-specific ADAT3 N-terminal domain. This domain can rotate with respect to the ADAT catalytic domain to present and position the tRNA anticodon-stem-loop correctly in ADAT2 active site. A founder mutation in the ADAT3 N-terminal domain, which causes intellectual disability, does not affect tRNA binding despite the structural changes it induces but most likely hinders optimal presentation of the tRNA anticodon-stem-loop to ADAT2.
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O'Donoghue, Patrick, and Zaida Luthey-Schulten. "On the Evolution of Structure in Aminoacyl-tRNA Synthetases." Microbiology and Molecular Biology Reviews 67, no. 4 (December 2003): 550–73. http://dx.doi.org/10.1128/mmbr.67.4.550-573.2003.

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SUMMARY The aminoacyl-tRNA synthetases are one of the major protein components in the translation machinery. These essential proteins are found in all forms of life and are responsible for charging their cognate tRNAs with the correct amino acid. The evolution of the tRNA synthetases is of fundamental importance with respect to the nature of the biological cell and the transition from an RNA world to the modern world dominated by protein-enzymes. We present a structure-based phylogeny of the aminoacyl-tRNA synthetases. By using structural alignments of all of the aminoacyl-tRNA synthetases of known structure in combination with a new measure of structural homology, we have reconstructed the evolutionary history of these proteins. In order to derive unbiased statistics from the structural alignments, we introduce a multidimensional QR factorization which produces a nonredundant set of structures. Since protein structure is more highly conserved than protein sequence, this study has allowed us to glimpse the evolution of protein structure that predates the root of the universal phylogenetic tree. The extensive sequence-based phylogenetic analysis of the tRNA synthetases (Woese et al., Microbiol. Mol. Biol. Rev. 64:202-236, 2000) has further enabled us to reconstruct the complete evolutionary profile of these proteins and to make connections between major evolutionary events and the resulting changes in protein shape. We also discuss the effect of functional specificity on protein shape over the complex evolutionary course of the tRNA synthetases.
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Strobel, M. C., and J. Abelson. "Effect of intron mutations on processing and function of Saccharomyces cerevisiae SUP53 tRNA in vitro and in vivo." Molecular and Cellular Biology 6, no. 7 (July 1986): 2663–73. http://dx.doi.org/10.1128/mcb.6.7.2663-2673.1986.

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The Saccharomyces cerevisiae leucine-inserting amber suppressor tRNA gene SUP53 (a tRNALeu3 allele) was used to investigate the relationship between precursor tRNA structure and mature tRNA function. This gene encodes a pre-tRNA which contains a 32-base intron. The mature tRNASUP53 contains a 5-methylcytosine modification of the anticodon wobble base. Mutations were made in the SUP53 intron. These mutant genes were transcribed in an S. cerevisiae nuclear extract preparation. In this extract, primary tRNA gene transcripts are end-processed and base modified after addition of cofactors. The base modifications made in vitro were examined, and the mutant pre-tRNAs were analyzed for their ability to serve as substrates for partially purified S. cerevisiae tRNA endonuclease and ligase. Finally, the suppressor function of these mutant tRNA genes was assayed after their integration into the S. cerevisiae genome. Mutant analysis showed that the totally intact precursor tRNA, rather than any specific sequence or structure of the intron, was necessary for efficient nonsense suppression by tRNASUP53. Less efficient suppressor activity correlated with the absence of the 5-methylcytosine modification. Most of the intron-altered precursor tRNAs were successfully spliced in vitro, indicating that modifications are not critical for recognition by the tRNA endonuclease and ligase.
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Dissertations / Theses on the topic "TRNA Structure"

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Boonyalai, Nonlawat. "Lysyl-tRNA synthetase : structure-function studies." Thesis, Imperial College London, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.429379.

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Lorber, Bernard. "Contribution a l'etude du systeme aspartyl-trna synthetase-trna**(asp) chez la levure saccharomyces cerevisiae." Université Louis Pasteur (Strasbourg) (1971-2008), 1987. http://www.theses.fr/1987STR13049.

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Swinehart, William E. Jr. "A Biochemical Investigation of Saccharomyces cerevisiae Trm10 and Implications of 1-methylguanosine for tRNA Structure and Function." The Ohio State University, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=osu1429867956.

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Nassar, Nicolas. "Structure de la seryl-tRNA synthétase de Escherichia coli à 2. 5 [angström] de résolution." Grenoble 1, 1992. http://www.theses.fr/1992GRE10162.

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La seryl-trna synthetase, serrs, est une enzyme qui catalyse l'attachement de la serine sur l'un des cinq trna specifiques de cet acide amine ainsi que sur le trna specifique de la selenocysteine en presence d'atp et d'ions mg. L'enzyme de escherichia coli (2430 residus) a ete cristallisee en presence d'ammonium sulfate et d'un lot special d'octyl-glucoside et la structure resolue a 2. 5a de resolution par la methode du remplacement isomorphe (mir). Trois cristaux derives de dy, hg et u ont ete necessaires pour calculer les phases mir. Quinze cycles d'aplatissement de solvant de cette premiere carte de densite electronique calculee a 2. 8a, combine a une extension des phases a 2. 5a a permis d'ameliorer la qualite des phases jusqu'a 2. 8a. Par contre les phases calculees par cette methode entre 2. 8 et 2. 5a sont de qualite mediocre. Cette nouvelle carte a permis le trace du premier squelette de l'assignement des differents residus de la serrs. Ce modele a ete affine par dynamique moleculaire et par moindres carres contre les donnees de diffraction x jusqu'a un facteur r cristallographique de 0. 183 et une excellente geometrie. La serrs peut etre divisee en deux domaines distincts: un domaine n-terminal comprenant les 100 premiers residus qui se replient en 4 helices dont deux forment une super helice a double brins de 60a de longueur. Le role de ce domaine serait d'interagir et de reconnaitre le trna; et un second domaine c-terminal forme par le reste de l'enzyme et qui se replie autour d'une cavite formee par sept brins beta antiparalleles. Ce domaine contient les trois motifs 1,2 et 3 communs aux synthetases de classe ii a laquelle la serrs appartient. Le motif 1, qui ne fait pas partie du tonneau beta mais plutot de l'insertion entre les brins a1 et a7, est implique dans l'interaction entre les deux sous-unites du dimere. Les motifs 2 et 3, qui constituent deux brins du tonneau beta, sont impliques dans la fixation de l'atp et l'activation de la serine meme si atp et serine n'ont jamais ete identifies dans la carte de densite electronique. Ce domaine contient une extra molecule non encore chimiquement identifiee et qui pourrait etre responsable de la cristallisation. Une nouvelle forme cristalline de la serrs a ete obtenue en presence d'hexyl-heptyl- et octyl-glucoside et d'ammonium sulfate. Ces cristaux sont orthorhombiques mais ont un faible pouvoir diffractant. La structure de la serrs differe de celles de la metrs, tyrs et glnrs toutes trois de classe i et construites autour d'un motif apparente au motif de rossmann. Cette difference dans le repliement conforte la nouvelle classification des synthetases en deux classes distinctes
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Agyeman, Akwasi. "T box antiterminator-tRNA recognition elements /." View abstract, 2007. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqdiss&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:3266062.

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Desogus, Gianluigi. "Structural studies of lysyl-tRNA synthetases and DNA primases." Thesis, Imperial College London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.369258.

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Mejdoub, Hafedh. "Aspartyl-trna synthetase cytoplasmique de levure : structure primaire et domaines accessibles." Université Louis Pasteur (Strasbourg) (1971-2008), 1987. http://www.theses.fr/1987STR13042.

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Mejdoub, Hafedh. "Aspartyl-tRNA synthétase cytoplasmique de levure structure primaire et domaines accessibles /." Grenoble 2 : ANRT, 1987. http://catalogue.bnf.fr/ark:/12148/cb37608053w.

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Cacan, Ercan. "Evolutionary synthetic biology: structure/function relationships within the protein translation system." Thesis, Georgia Institute of Technology, 2011. http://hdl.handle.net/1853/45838.

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Production of mutant biological molecules for understanding biological principles or as therapeutic agents has gained considerable interest recently. Synthetic genes are today being widely used for production of such molecules due to the substantial decrease in the costs associated with gene synthesis technology. Along one such line, we have engineered tRNA genes in order to dissect the effects of G:U base-pairs on the accuracy of the protein translation machinery. Our results provide greater detail into the thermodynamic interactions between tRNA molecules and an Elongation Factor protein (termed EF-Tu in bacteria and eEF1A in eukaryotes) and how these interactions influence the delivery of aminoacylated tRNAs to the ribosome. We anticipate that our studies not only shed light on the basic mechanisms of molecular machines but may also help us to develop therapeutic or novel proteins that contain unnatural amino acids. Further, the manipulation of the translation machinery holds promise for the development of new methods to understand the origins of life. Along another line, we have used the power of synthetic biology to experimentally validate an evolutionary model. We exploited the functional diversity contained within the EF-Tu/eEF1A gene family to experimentally validate the model of evolution termed ‘heterotachy’. Heterotachy refers to a switch in a site’s mutational rate class. For instance, a site in a protein sequence may be invariant across all bacterial homologs while that same site may be highly variable across eukaryotic homologs. Such patterns imply that the selective constraints acting on this site differs between bacteria and eukaryotes. Despite intense efforts and large interest in understanding these patterns, no studies have experimentally validated these concepts until now. In the present study, we analyzed EF-Tu/eEF1A gene family members between bacteria and eukaryotes to identify heterotachous patterns (also called Type-I functional divergence). We applied statistical tests to identify sites possibly responsible for biomolecular functional divergence between EF-Tu and eEF1A. We then synthesized protein variants in the laboratory to validate our computational predictions. The results demonstrate for the first time that the identification of heterotachous sites can be specifically implicated in functional divergence among homologous proteins. In total, this work supports an evolutionary synthetic biology paradigm that in one direction uses synthetic molecules to better understand the mechanisms and constraints governing biomolecular behavior while in another direction uses principles of molecular sequence evolution to generate novel biomolecules that have utility for industry and/or biomedicine.
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Perreau, Victoria M. "Genomic organisation and structure of a novel seryl-tRNA from Candida albicans." Thesis, University of Kent, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.242889.

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Books on the topic "TRNA Structure"

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Dieter, Söll, and RajBhandary Uttam, eds. tRNA: Structure, biosynthesis, and function. Washington, D.C: ASM Press, 1995.

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Venegoni, Carlotta. La chiesa parrocchiale della Natività della Beata Vergine Maria di Trana. Cantalupa (Torino): Effatà editrice, 2021.

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Questionnaire design: How to plan, structure and write survey material for effective market research. 2nd ed. London: Kogan Page, 2008.

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Knoll, Franz, and Thomas Vogel. Design for Robustness. Zurich, Switzerland: International Association for Bridge and Structural Engineering (IABSE), 2009. http://dx.doi.org/10.2749/sed011.

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<p>Robustness is the ability to survive unforeseen circum-stances without undue damage or loss of function. It has become a requirement expressed in modern building codes, mostly without much advice as to how it can be achieved. Engineering has developed some approaches based on tra-ditional practice as well as recent insight. However, know-ledge about robustness remains scattered and ambiguous, making it difficult to apply to many specific cases.<p> The authors' attempt to collect and review elements, methods and strategies toward structural robustness, using a holistic, almost philosophical approach. This leads to a set of consid-erations to guide selection and implementation of measures in specific cases, followed by a collection of applications and examples from the authors practice.<p>The world, engineering and construction are imperfect and not entirely predictable. Robustness provides a measure of structural safety beyond traditional codified design rules.
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Soll, Dieter. Trna: Structure, Biosynthesis, and Function. ASM Press, 1995.

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Soll, Dieter, and Uttam L. RajBhandary. TRNA: Structure, Biosynthesis, and Function. Wiley & Sons, Limited, John, 2014.

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Shen, Wenyan *. Studies of the structure and function of "Bacillus subtilis" tRNAs in "Escherichia coli". 1991.

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Sanders, Kyle, Craig Miller, Ricardo Yamada, and Marcelo Guimaraes. Transradial Access Technique. Edited by S. Lowell Kahn, Bulent Arslan, and Abdulrahman Masrani. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199986071.003.0058.

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Transradial access (TRA) competency can be rapidly achieved by the experienced interventionist. Statistically significant reductions in bleeding and other access site complications have been shown in randomized and meta-analysis studies when comparing TRA to both brachial and femoral artery access. Despite accumulating data, vascular interventional radiologists have been hesitant to adopt TRA for a variety of reasons. However, TRA offers distal dual blood supply, easily achievable hemostasis, and no adjacent critical structures. Other advantages of TRA are safer endovascular approach concomitant with earlier ambulation, improved patient comfort, decreased length of stay, as well as potential for cost savings. This chapter discusses the TRA technique, applications, challenges, and potential complications.
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Book chapters on the topic "TRNA Structure"

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Meinnel, Thierry, Yves Mechulam, and Sylvain Blanquet. "Aminoacyl-tRNA Synthetases: Occurrence, Structure, and Function." In tRNA, 251–92. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555818333.ch14.

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Inokuchi, Hachiro, and Fumiaki Yamao. "Structure and Expression of Prokaryotic tRNA Genes." In tRNA, 17–30. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555818333.ch3.

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Baron, Christian, and August Böck. "The Selenocysteine-Inserting tRNA Species: Structure and Function." In tRNA, 529–44. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555818333.ch26.

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Sherman, Joyce M., M. John Rogers, and Dieter Söll. "Recognition in the Glutamine tRNA System: from Structure to Function." In tRNA, 395–409. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555818333.ch19.

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Marquéz, Viter, Knud H. Nierhaus, Luís Ribas de Pouplana, and Pauls Schimmel. "tRNA and Synthetases." In Protein Synthesis and Ribosome Structure, 145–84. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/3527603433.ch4.

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Maréchal-Drouard, L., P. Guillemaut, H. Pfitzingzer, and J. H. Weil. "Chloroplast tRNAs and tRNA genes: structure and function." In The Translational Apparatus of Photosynthetic Organelles, 45–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75145-5_4.

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Nierhaus, Knud H. "tRNA Locations on the Ribosome." In Protein Synthesis and Ribosome Structure, 207–17. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/3527603433.ch6.

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Alfonzo, Juan D. "Editing of tRNA for Structure and Function." In Nucleic Acids and Molecular Biology, 33–50. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-73787-2_2.

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Klebe, Gerhard. "Structure-Based Design of Trna-Guanine Transglycosylase Inhibitors." In NATO Science for Peace and Security Series A: Chemistry and Biology, 103–20. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-2339-1_7.

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Grosjean, H., C. Houssier, and R. Cedergren. "Anticodon-Anticodon Interactions and tRNA Sequence Comparison: Approaches to Codon Recognition." In Structure and Dynamics of RNA, 161–74. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5173-3_14.

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Conference papers on the topic "TRNA Structure"

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Tahami, Amid, Mohammadreza Gholikhani, Reza Khalili, and Samer Dessouky. "Application of Thermoelectric Technology in Sustainable Pavement Structures." In Tran-SET 2020. Reston, VA: American Society of Civil Engineers, 2021. http://dx.doi.org/10.1061/9780784483305.002.

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Ahmed, Hassan, Ilerioluwa Giwa, Daniel E. Game, Marc Hebert, Hassan Noorvand, Gabriel A. Arce, Marwa Hassan, and Ali Kazemian. "Studying Steel Fiber Reinforcement for 3D Printed Elements and Structures." In Tran-SET 2022. Reston, VA: American Society of Civil Engineers, 2022. http://dx.doi.org/10.1061/9780784484609.032.

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Majlesi, Arsalan, Reza Nasouri, Adnan Shahriar, Arturo Montoya, and Adolfo Matamoros. "Structural Vulnerability of Coastal Bridges under a Variety of Hydrodynamic Conditions." In Tran-SET 2020. Reston, VA: American Society of Civil Engineers, 2021. http://dx.doi.org/10.1061/9780784483305.012.

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Varbel, Jordan M., Elsy Y. Flores, William K. Toledo, Craig M. Newtson, and Brad D. Weldon. "Structural Testing of Ultra-High Performance Concrete Shear Keys in Concrete Bridge Superstructures." In Tran-SET 2020. Reston, VA: American Society of Civil Engineers, 2021. http://dx.doi.org/10.1061/9780784483305.027.

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Li, Wendi, Wei Wei, Xiaoye Qu, Xian-Ling Mao, Ye Yuan, Wenfeng Xie, and Dangyang Chen. "TREA: Tree-Structure Reasoning Schema for Conversational Recommendation." In Proceedings of the 61st Annual Meeting of the Association for Computational Linguistics (Volume 1: Long Papers). Stroudsburg, PA, USA: Association for Computational Linguistics, 2023. http://dx.doi.org/10.18653/v1/2023.acl-long.167.

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Bastola, Nitish R., Mena I. Souliman, and Samer Dessouky. "Structural Health Assessment of Pavement Sections in the Southern Central States Using FWD Parameters." In Tran-SET 2022. Reston, VA: American Society of Civil Engineers, 2022. http://dx.doi.org/10.1061/9780784484609.023.

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Ibrahim, Habib, and Fatih Ozkaynak. "A Substitution-Box Structure Based on Crowd Supply Infinite Noise TRNG." In 2021 9th International Symposium on Digital Forensics and Security (ISDFS). IEEE, 2021. http://dx.doi.org/10.1109/isdfs52919.2021.9486317.

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Choe, Jun-Yeong, and Kyung-Wook Shin. "A Self-Timed Ring based TRNG with Feedback Structure for FPGA Implementation." In 2020 International Conference on Electronics, Information, and Communication (ICEIC). IEEE, 2020. http://dx.doi.org/10.1109/iceic49074.2020.9051375.

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Janbakhsh, Lyndsie, Justin Anderson, and Kevin Kriete. "Innovative Design for the Merchants Bridge West Approach Reconstruction for TRRA in St. Louis, MO." In Geotechnical and Structural Engineering Congress 2016. Reston, VA: American Society of Civil Engineers, 2016. http://dx.doi.org/10.1061/9780784479742.068.

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Almadhaji, Ahmed, Mohammed Saeed, Hitham Ibrahim, Anas Ahmed, and Ragaei Maher. "Enhancing Rheological Properties and Reduction of Total Acid Number of a Heavy Crude Oil Using Ethanol and Trona." In SPE/IATMI Asia Pacific Oil & Gas Conference and Exhibition. SPE, 2021. http://dx.doi.org/10.2118/205621-ms.

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Abstract:
Abstract One of Sudanese fields has a heavy crude oil which has a high Total Acid Number (TAN) and high viscosity, can cause a lot of problems in production operation, transport, and storage facilities. The effect of ethanol dilution on the rheological properties of crude (especially the kinematic viscosity) was studied and presented. Moreover, the consequence of blending Trona (NaHCO3.Na2CO3) with a specified amount of Ethanol in the crude can reduce (TAN) to acceptable limits for solving corrosion and flowability problems. The approach is based on the experiments and laboratory works on the crude's samples after blending with a certain amount of Trona and Ethanol. It depends on the results of apparatuses, that are used to measure the samples, for instance, Calibrated glass capillary viscometer and ASTM D664 titration volume Total Acid Number tester which are employed to get the values of kinematic viscosity and TAN, respectively. The tests are established with crude have kinematic viscosity (187 cst) at temperature 75°C and TAN almost (8.51). While increasing the dosage of Trona at the ambient temperature (38°C) with the certain mass percentage of Ethanol (5%), TAN is decreased from (8.51 to 4.00 mgKOH/g). Also, the kinematic viscosity is declined from (187 cst to 96.75 cst) after increasing the volume of Ethanol at 75°C. These outcomes indicated that Ethanol could reduce Sudanese heavy crude's viscosity, and the Trona could decrease the TAN. This reduction occurred due to Ethanol dilution. The Ethanol molecules disturb the molecular structure of the crude, which forms polar bond within the hydrocarbon chain that leads to lower the friction between molecules of hydrocarbon in the crude. Also, Trona shrinks TAN because the Hydroxide ions (OH+) that founded in Trona neutralize the Hydrogen ions (H−) in Naphthenic acid in Sudanese heavy crude. This study can be summarized in the ability to solve the difficulty of transporting and processing the heavy crude oil in refineries; maintains the quality of the crude while utilizing it with friendly environmental materials and low cost.
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