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Related Concept Videos

tRNA Activation02:26

tRNA Activation

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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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tRNA Activation02:26

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Improving Translational Accuracy02:07

Improving Translational Accuracy

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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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Drug toxicity: Drug–Drug Interaction01:30

Drug toxicity: Drug–Drug Interaction

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Drug–drug interactions can precipitate toxicity through multiple mechanisms. Absorption interactions alter how drugs enter the body, exemplified when ranitidine increases the absorption of basic drugs, while cholestyramine decreases the levels of propranolol. Protein binding interactions occur when drugs share the same binding sites on plasma proteins. Drugs like aspirin and warfarin, when bound in excess, can lead to increased free drug concentrations, enhancing the potential for...
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Pharmacokinetics: Drug–Drug Interactions01:25

Pharmacokinetics: Drug–Drug Interactions

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Drug interactions occur when the pharmacological effect of one drug is altered by another substance, either enhancing or diminishing its activity. The drug whose activity is altered is known as the object drug, and the substance causing the alteration is called the agent drug or the precipitant. The net effects of these interactions are mostly undesirable, leading to decreased effectiveness or increased adverse effects. In rare cases, interactions can be beneficial, such as the enhanced...
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Bioequivalence of Drugs: Drugs with Multiple Indications01:09

Bioequivalence of Drugs: Drugs with Multiple Indications

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The concept of therapeutic equivalence (TE) in drugs with multiple indications is complex. A generic drug may be therapeutically equivalent to a brand-name product for one specific indication, but this doesn't necessarily mean it's equivalent for all other indications. Evidence of TE in one patient group and bioequivalence shown in healthy volunteers can support—but not confirm—TE for other indications. However, definitive proof requires individual clinical studies for each...
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Genome-wide Analysis of Aminoacylation Charging Levels of tRNA Using Microarrays
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Genome-wide Analysis of Aminoacylation Charging Levels of tRNA Using Microarrays

Published on: June 18, 2010

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Drugging tRNA aminoacylation.

Joanne M Ho1, Erol Bakkalbasi2, Dieter Söll3,4

  • 1a Department of BioSciences , Rice University , Houston , TX , United States.

RNA Biology
|January 19, 2018
PubMed
Summary
This summary is machine-generated.

Targeting bacterial tRNA aminoacylation offers a potent antimicrobial approach. Understanding the coevolved specificity between aminoacyl-tRNA synthetases (aaRSs) and tRNA in pathogens aids novel drug design.

Keywords:
Aminoacylationaminoacyl tRNA synthetasesantibiotic targetsantibioticsantimicrobialsdrug developmentdrug targetstransfer RNAtranslation inhibitors

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In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 Ehmeth Enzyme
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An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity
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Area of Science:

  • Microbiology
  • Biochemistry
  • Drug Discovery

Background:

  • Inhibiting tRNA aminoacylation is a validated antimicrobial strategy by disrupting protein synthesis.
  • Mupirocin exemplifies approved aminoacylation inhibitors, targeting bacterial isoleucyl-tRNA synthetase.
  • Developing new inhibitors requires avoiding human protein synthesis interference.

Purpose of the Study:

  • To review known aminoacylation inhibitors.
  • To analyze determinants of aminoacyl-tRNA synthetase (aaRS)-tRNA specificity.
  • To explore the potential for antimicrobial drug development.

Main Methods:

  • Literature review of existing aminoacylation inhibitors.
  • Analysis of amino acid residues in aaRSs and tRNA nucleotides.
  • Examination of aaRS-tRNA recognition and coevolution.

Main Results:

  • The aaRS-tRNA interaction is a coevolved system crucial for aminoacylation specificity.
  • Specificity determinants in pathogens often differ from those in humans.
  • These differences present opportunities for selective drug targeting.

Conclusions:

  • The coevolution of aaRSs and tRNA provides a basis for developing pathogen-specific inhibitors.
  • Exploiting divergent recognition mechanisms can lead to novel antimicrobial agents.
  • This strategy offers a promising avenue for combating bacterial infections.