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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...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
tRNA Activation02:26

tRNA Activation

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...
tRNA Activation02:26

tRNA Activation

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...
RNA Structure01:19

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The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
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Published on: February 25, 2011

Exploring GpG bases next to anticodon in tRNA subsets.

Thangavelu Srinivasan1, Kubendiran Kumaran, Rajendran Selvakumar

  • 1DST-FIST Bioinformatics & Principal Investigator, School of Genomics, Department of Advanced Zoology and Biotechnology, Loyola College, Chennai - 600 034, Tamil Nadu, India.

Bioinformation
|July 13, 2013
PubMed
Summary

Transfer RNA (tRNA) methylation at position 37 (m1G37) is crucial for protein synthesis. This study proposes that m1G37 modification may occur at various positions (36-40) near the anticodon in tRNAs across different species.

Keywords:
AnticodonCodonm1G modificationtRNAs

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Transfer RNA (tRNA) modifications are essential for stability and accurate protein synthesis.
  • A conserved methylation, m1G37, occurs next to the anticodon loop in tRNAs, catalyzed by TrmD.
  • Guanosine residues near the anticodon are found in various positions across different domains of life.

Purpose of the Study:

  • To investigate the potential for m1G37 modification at positions beyond the 37th.
  • To explore the evolutionary conservation and variability of guanosine residue positions near the tRNA anticodon.
  • To propose a broader scope for m1G37 modification in tRNA function.

Main Methods:

  • Bioinformatic analysis of tRNA sequences across bacteria, archaea, and eukaryotes.
  • Comparative genomics to identify conserved and variable guanosine residue positions.
  • Literature review on tRNA methyltransferases and their substrates.

Main Results:

  • Guanosine residues are present at positions 36, 37, 38, 39, and 40 in various tRNA subsets across species.
  • In bacteria, G residues are typically at positions 37 and 38, with exceptions at 36 and 39.
  • Archaea and eukaryotes exhibit a wider distribution of G residues near the anticodon.

Conclusions:

  • The m1G37 modification is potentially feasible at multiple positions (36-40) adjacent to the tRNA anticodon.
  • Methylation near the anticodon may not be restricted by the identity of the third base of the anticodon.
  • This finding expands our understanding of tRNA modification diversity and its functional implications.