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Related Concept Videos

LTR Retrotransposons03:08

LTR Retrotransposons

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LTR retrotransposons are class I transposable elements with long terminal repeats flanking an internal coding region. These elements are less abundant in mammals compared to other class I transposable elements. About 8 percent of human genomic DNA comprises LTR retrotransposons. Some of the common examples of LTR retrotransposons are Ty elements in yeast and Copia elements in Drosophila.
The internal coding region of LTR retrotransposons and their mechanism of transposition closely resembles a...
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Non-LTR Retrotransposons03:18

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As the name suggests, non-LTR retrotransposons lack the long terminal repeats characteristic of the LTR retrotransposons. Additionally, both LTR and non-LTR retrotransposons use distinct mechanisms of mobilization. Non-LTR retrotransposons are further divided into two classes - Long interspersed nuclear elements (LINEs) and short interspersed nuclear elements (SINEs), both of which occur abundantly in most mammals, including humans. Some of the active non-LTR retrotransposons in humans are L1...
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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 Activation

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Fixing Double-strand Breaks02:04

Fixing Double-strand Breaks

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The double-stranded structure of DNA has two major advantages. First, it serves as a safe repository of genetic information where one strand serves as the back-up in case the other strand is damaged. Second, the double-helical structure can be wrapped around proteins called histones to form nucleosomes, which can then be tightly wound to form chromosomes. This way, DNA chains up to 2 inches long can be contained within microscopic structures in a cell. A double-stranded break not only damages...
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Fixing Double-strand Breaks02:04

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Related Experiment Video

Updated: Feb 8, 2026

In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 Ehmeth Enzyme
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In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 Ehmeth Enzyme

Published on: October 19, 2010

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Tie-Break: Host and Retrotransposons Play tRNA.

Andrea J Schorn1, Rob Martienssen2

  • 1Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.

Trends in Cell Biology
|June 24, 2018
PubMed
Summary

Small regulatory RNAs called tRNA fragments (tRFs) target mobile genetic elements like LTR-retrotransposons. These 3'-derived tRFs inhibit retrotransposon activity, potentially protecting genome stability.

Keywords:
LTR-retrotransposonprimer binding siteretrovirussmall RNAtRFtRNA

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Genome-wide Analysis of Aminoacylation Charging Levels of tRNA Using Microarrays
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Area of Science:

  • Molecular Biology
  • Genetics
  • RNA Biology

Background:

  • tRNA fragments (tRFs) are small regulatory RNAs with diverse biological roles.
  • Long terminal repeat (LTR)-retroelements utilize tRNA 3"-ends for reverse transcription priming.
  • tRFs have emerged as key regulators in RNA interference (RNAi) pathways.

Purpose of the Study:

  • To investigate the role of 3"-derived tRFs in targeting LTR-retroelements.
  • To elucidate the mechanism by which tRFs inhibit retrotransposon mobility and reverse transcription.
  • To understand the significance of tRFs in maintaining genome stability during epigenetic reprogramming.

Main Methods:

  • Analysis of tRNA fragment sequences and their complementarity to LTR-retroelement primer binding sites.
  • Investigating the targeting of LTR-retroelements by tRFs via the RNAi pathway.
  • Assessing the impact of tRFs on retrotransposon reverse transcription and mobility.

Main Results:

  • 3"-derived tRFs exhibit perfect complementarity to the primer binding site (PBS) of LTR-retroelements.
  • tRFs effectively target LTR-retroviruses and transposons for RNAi-mediated degradation.
  • tRFs inhibit LTR-retroelement mobility by blocking reverse transcription, particularly during epigenetic reprogramming.

Conclusions:

  • 3"-tRFs represent a conserved mechanism to suppress abundant and diverse LTR-retrotransposons.
  • The interaction between tRFs and the tRNA primer binding site (PBS) is crucial for genome defense.
  • tRFs may serve as an ancient link connecting RNAi, transposon control, and genome integrity across various cell types.