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Related Concept Videos

Improving Translational Accuracy02:07

Improving Translational Accuracy

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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Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
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The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
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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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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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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Published on: August 9, 2019

RNA aptamers to translational components.

Yoshikazu Nakamura1, Kei Endo, Hironori Adachi

  • 1Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo, Tokyo, Japan.

Progress in Molecular Biology and Translational Science
|April 9, 2010
PubMed
Summary

RNA aptamers offer a promising therapeutic avenue by targeting proteins, including human translation initiation factors. Their high affinity arises from capturing protein conformation, showcasing

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Area of Science:

  • Biochemistry and Molecular Biology
  • RNA Therapeutics
  • Drug Discovery

Background:

  • Functional RNAs and RNA aptamers are expanding therapeutic applications.
  • RNA aptamers are short, folded nucleic acid molecules selected in vitro for high target affinity.
  • They can suppress target molecule activity.

Purpose of the Study:

  • To summarize RNA aptamers selected against human translation initiation factors.
  • To highlight their potential for recognizing and inhibiting target proteins.
  • To explore the concept of 'RNA plasticity' in aptamer design.

Main Methods:

  • In vitro selection of RNA aptamers against specific protein targets.
  • Characterization of aptamer-protein interactions.
  • Analysis of aptamer binding mechanisms.

Main Results:

  • RNA aptamers were successfully selected against human translation initiation factors.
  • These aptamers exhibit high affinity and inhibitory potential towards their target proteins.
  • Aptamer binding is achieved by recognizing the protein's global conformation, not just RNA-binding motifs.

Conclusions:

  • RNA aptamers demonstrate significant potential as therapeutic agents.
  • The concept of 'RNA plasticity' underpins the ability of RNA to form diverse tertiary structures for high-affinity binding.
  • RNA aptamers may offer an alternative or superior therapeutic modality compared to antibodies.